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Pyruvate dehydrogenase kinase

2026-08-27T10:02:18Z

Michal Harel:

<StructureSection load='' size='350' side='right' caption='Human pyruvate dehydrogenase kinase isozyme 4 dimer complex with AMPPNP and Mg+2 ion (green) (PDB entry [[2e0a]])' scene='48/485629/Cv/1'>
__TOC__

== Function ==
'''Pyruvate dehydrogenase kinase''' (PDK) is part of the pyruvate dehydrogenase complex. This complex is located in the mitochondria and converts pyruvate to acetyl-CoA as part of the citric acid cycle. PDK phosphphorylates serine residues on pyruvate dehydrogenase using ATP. There are 4 isozymes of PDK. The isozymes differ in length, activity and phosphorylation sites<ref>PMID:11486000</ref>.
*'''PDK1''' is abundant in heart cells. PDK1 expression was found to predict future major adverse cardiovascular events<ref>PMID:36866436</ref>.
*'''PDK2''' is abundant in mitochondria.
*'''PDK3''' is abundant in testis.
*'''PDK4''' is abundant in muscle and heart. It is important during starvation for regulation of pyruvate dehydrogenate complex activity and glucose homoeostasis<ref>PMID:16606348</ref>.

== Relevance ==
Inhibition of PDK decreases the damage caused by heart ischemia and are used in diabetes and cancer patients<ref>PMID:17310282</ref><ref>PMID:23471124</ref>.

== Structural highlights ==
<scene name='48/485629/Cv/11'>The active site cleft of PDK4 binds AMPPNP</scene><ref>PMID:21904029</ref>. Water molecules are shown as red spheres. <scene name='48/485629/Cv/12'>Mg coordination site</scene>.
</StructureSection>
==3D structures of pyruvate dehydrogenase kinase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*PDK isozyme 1

**[[2q8f ]]– hPDK1 – human 
**[[2q8g]] – hPDK1 + drug 
**[[2q8h]] – hPDK1 + dichloro-acetic acid

*PDK isozyme 2

**[[2btz]] – hPDK2 
**[[2bu2]] – hPDK2 + benzonitrile derivative + ATP 
**[[2bu5]] - hPDK2 + benzonitrile derivative 
**[[2bu6]] - hPDK2 + propanamide derivative 
**[[2bu7]] - hPDK2 + acetamide derivative 
**[[2bu8]] - hPDK2 + dichloro-acetic acid + ADP 
**[[4mp2]], [[4mp7]], [[4mpc]], [[4mpe]], [[4mpn]], [[4v25]], [[4v26]], [[5j6a]], [[5j71]], [[5m4k]], [[5m4m]], [[5m4n]], [[5m4p]], [[6lil]], [[6lio]], [[6lin]], [[6tmp]], [[6tmq]], [[6tmz]], [[6tn0]], [[6tn2]], [[7eas]], [[7ebh]], [[7vbu]], [[7vbv]], [[7vbx]], [[8zm1]], [[8zm2]], [[9m3o]], [[9m3p]], [[9m3r]], [[9m3t]], [[9m3u]] – hPDK2 + inhibitor 
**[[3crk]], [[3crl]] – hPDK2 + pyruvate dehydrogenase E2 
**[[1jm6]] – PDK2 + ADP – rat 

*PDK isozyme 3

**[[1y8n]], [[1y8o]], [[1y8p]], [[2pnr]] – hPDK3 + acetyltransferase component of pyruvate dehydrogenase complex 
**[[2q8i]] – hPDK3 + radicicol

*PDK isozyme 4

**[[2e0a]] – hPDK4 + AMPPNP 
**[[2zkj]], [[3d2r]] – hPDK4 + ADP 
**[[7ea0]], [[7eat]], [[7ebb]], [[7ebg]] – hPDK4 + inhibitor 
**[[2zdx]], [[2zdy]] – hPDK4 (mutant) + inhibitor
}}
== References ==
<references/>

[[Category: Topic Page]]

Pyruvate dehydrogenase kinase

2026-08-27T09:55:52Z

Michal Harel:

<StructureSection load='' size='350' side='right' caption='Human pyruvate dehydrogenase kinase isozyme 4 dimer complex with AMPPNP and Mg+2 ion (green) (PDB entry [[2e0a]])' scene='48/485629/Cv/1'>
__TOC__

== Function ==
'''Pyruvate dehydrogenase kinase''' (PDK) is part of the pyruvate dehydrogenase complex. This complex is located in the mitochondria and converts pyruvate to acetyl-CoA as part of the citric acid cycle. PDK phosphphorylates serine residues on pyruvate dehydrogenase using ATP. There are 4 isozymes of PDK. The isozymes differ in length, activity and phosphorylation sites<ref>PMID:11486000</ref>.
*'''PDK1''' is abundant in heart cells. PDK1 expression was found to predict future major adverse cardiovascular events<ref>PMID:36866436</ref>.
*'''PDK2''' is abundant in mitochondria.
*'''PDK3''' is abundant in testis.
*'''PDK4''' is abundant in muscle and heart. It is important during starvation for regulation of pyruvate dehydrogenate complex activity and glucose homoeostasis<ref>PMID:16606348</ref>.

== Relevance ==
Inhibition of PDK decreases the damage caused by heart ischemia and are used in diabetes and cancer patients<ref>PMID:17310282</ref><ref>PMID:23471124</ref>.

== Structural highlights ==
<scene name='48/485629/Cv/11'>The active site cleft of PDK4 binds AMPPNP</scene><ref>PMID:21904029</ref>. Water molecules are shown as red spheres. <scene name='48/485629/Cv/12'>Mg coordination site</scene>.
</StructureSection>
==3D structures of pyruvate dehydrogenase kinase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*PDK isozyme 1

**[[2q8f ]]– hPDK1 – human 
**[[2q8g]] – hPDK1 + drug 
**[[2q8h]] – hPDK1 + dichloro-acetic acid

*PDK isozyme 2

**[[2btz]] – hPDK2 
**[[2bu2]] – hPDK2 + benzonitrile derivative + ATP 
**[[2bu5]] - hPDK2 + benzonitrile derivative 
**[[2bu6]] - hPDK2 + propanamide derivative 
**[[2bu7]] - hPDK2 + acetamide derivative 
**[[2bu8]] - hPDK2 + dichloro-acetic acid + ADP 
**[[4mp2]], [[4mp7]], [[4mpc]], [[4mpe]], [[4mpn]], [[4v25]], [[4v26]], [[5j6a]], [[5j71]], [[5m4k]], [[5m4m]], [[5m4n]], [[5m4p]], [[6lil]], [[6lio]], [[6lin]], [[6tmz]], [[6tmp]], [[6tmq]], [[6tn0]], [[6tn2]], [[7ebh]], [[7eas]], [[7vbu]], [[7vbv]], [[7vbx]] – hPDK2 + inhibitor 
**[[3crk]], [[3crl]] – hPDK2 + pyruvate dehydrogenase E2 
**[[1jm6]] – PDK2 + ADP – rat 

*PDK isozyme 3

**[[1y8n]], [[1y8o]], [[1y8p]], [[2pnr]] – hPDK3 + acetyltransferase component of pyruvate dehydrogenase complex 
**[[2q8i]] – hPDK3 + radicicol

*PDK isozyme 4

**[[2e0a]] – hPDK4 + AMPPNP 
**[[2zkj]], [[3d2r]] – hPDK4 + ADP 
**[[7ea0]], [[7eat]], [[7ebb]], [[7ebg]] – hPDK4 + inhibitor 
**[[2zdx]], [[2zdy]] – hPDK4 (mutant) + inhibitor
}}
== References ==
<references/>

[[Category: Topic Page]]

Pyruvate dehydrogenase 3D structures

2026-08-27T09:46:29Z

Michal Harel:

==3D structures of pyruvate dehydrogenase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyruvate dehydrogenase E1 domain

**[[3exe]] - hPDH E1 α + β subunits - human 
**[[1ni4]], [[6cfo]] – hPDH E1 α + β (mutant) subunits 
**[[2ozl]], [[3exg]], [[3exh]], [[3exi]], [[6cer]] - hPDH E1 α (mutant) + β subunits 
**[[3exf]] - hPDH E1 α (mutant) + β subunits + TDP 
**[[1ik6]] – PaPDH E1 β subunit – ''Pyrobaculum aerophilum'' 
**[[1l8a]], [[2g25]], [[2g67]], [[2iea]] – EcPDH E1 – ''Escherichia coli'' 
**[[3ey9]], [[3eya]] – EcPDH (cytochrome) 
**[[2qta]], [[3lpl]], [[3lq2]], [[3lq4]] - EcPDH E1 (mutant) 
**[[2qtc]] - EcPDH E1 (mutant) + phosphonolactylthiamin diphosphate 
**[[1rp7]] - EcPDH E1 + inhibitor 
**[[4qoy]] - EcPDH E1 + PDH E2 

*Pyruvate dehydrogenase E2 see [[Dihydrolipoyl transacetylase]] and [[Dihydrolipoamide acetyltransferase]]; Domains – peripheral-subunit binding (PSB) 118-170; lipoyl 179-282; catalytic 395-697

**[[3b8k]], [[6ct0]], [[8piu]] – hPDH E2 – Cryo EM 
**[[7uom]] – hPDH E2 catalytic domain – Cryo EM 
**[[8x03]] – PDH E2 – bovine - Cryo EM 
**[[8x03]], [[9j1w]] – PDH E2 – pig - Cryo EM 
**[[7bgj]], [[7ott]], [[7q5r]] – PDH E2 – ''Thermochaetoides thermophila'' – Cryo EM 
**[[7b9k]], [[8orb]] – EcPDH E2 catalytic domain – Cryo EM 
**[[4n72]], [[8osy]] – EcPDH E2 catalytic domain 
**[[1fyc]], [[1qjo]], [[2k7v]] – EcPDH E2 lipoyl domain - NMR 
**[[8oqj]] - EcPDH E2 PSB 
**[[1w4i]], [[1w4j]], [[1w4k]] - PaPDH E2 PSB - NMR 
**[[1eaa]], [[1eab]], [[1eac]], [[1ead]], [[1eae]], [[1eaf]] – AvPDH E2 catalytic domain – ''Azotobacter vinelandii'' 
**[[1iyu]], [[1iyv]] – AvPDH E2 1-79 – NMR 
**[[6zzi]], [[6zzm]] – CmPDH E2 catalytic domain – ''Corynebacterium mustelae'' 
**[[6zzj]] – CmPDH E2 catalytic domain + acetylCoA 
**[[6zzl]] – CgPDH E2 catalytic domain - Corynebacterium glutamicum 
**[[6zzk]] – CgPDH E2 catalytic domain + acetylCoA + dihydropolyamide 
**[[9y6t]], [[9y72]] – MtPDH E2 catalytic domain – Mycobacterium tuberculosis – Cryo EM 
**[[9y7v]] – MtPDH E2 catalytic domain + acetylCoA – Cryo EM 
**[[9ukz]] - BsPDH E2 catalytic domain – ''Bacillus stearothermophilus'' – Cryo EM 
**[[1w3d]], [[2pdd]], [[2pde]] - BsPDH E2 PSB - NMR 
**[[1lab]], [[1lac]] – BsPDH E2 lipoyl domain - NMR 

*Pyruvate dehydrogenase E1+E2

**[[1w85]], [[1w88]] - BsPDH E1 α + β subunits + PDH E2 peripheral-subunit binding domain 
**[[3duf]], [[3dv0]] - BsPDH E1 α + β subunits + PDH E2 
**[[3dva]] - BsPDH E1 α (mutant) + β subunits + PDH E2 
**[[9h1n]] - EcPDH E1 2-50 + PDH E2 315-380 

*Pyruvate dehydrogenase E3 or dihydrolipoyl dehydrogenase

**[[6h60]] – hPDH protein X – Cryo EM 
**[[1zy8]] – hPDH protein X + dihydrolipoyl dehydrogenase 
**[[2f5z]] - hPDH protein X (mutant) + dihydrolipoyl dehydrogenase 
**[[2f60]] - hPDH protein X (mutant) 
**[[2dnc]], [[2dne]] - hPDH protein X N terminal - NMR 
**[[2g25]] - hPDH protein X + phosphonolactylthiamin diphosphate 
**[[2g28]] - hPDH protein X (mutant) + phosphonolactylthiamin diphosphate 
**[[2eq8]] – TtPDH E3 – ''Thermus thermophilus'' 
**[[4jdr]], [[4jq9]] – EcPDH E3 
**[[1gjx]] – PDH E3 lipoyl domain – ''Neisseria meningitis'' – NMR 
**[[6zlm]], [[6zlo]], [[7r5m]], [[8ohs]] – NcPDH protein X + E2 – ''Neurospora crassa'' - Cryo EM 

*Pyruvate dehydrogenase E2+E3

**[[9h2i]] - EcPDH E2 catalytic domain + PDH E3 
}}

[[Category:Topic Page]]

Pyruvate dehydrogenase 3D structures

2026-08-27T09:44:48Z

Michal Harel:

==3D structures of pyruvate dehydrogenase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyruvate dehydrogenase E1 domain

**[[3exe]] - hPDH E1 α + β subunits - human 
**[[1ni4]], [[6cfo]] – hPDH E1 α + β (mutant) subunits 
**[[2ozl]], [[3exg]], [[3exh]], [[3exi]], [[6cer]] - hPDH E1 α (mutant) + β subunits 
**[[3exf]] - hPDH E1 α (mutant) + β subunits + TDP 
**[[1ik6]] – PaPDH E1 β subunit – ''Pyrobaculum aerophilum'' 
**[[1l8a]], [[2g25]], [[2g67]], [[2iea]] – EcPDH E1 – ''Escherichia coli'' 
**[[3ey9]], [[3eya]] – EcPDH (cytochrome) 
**[[2qta]], [[3lpl]], [[3lq2]], [[3lq4]] - EcPDH E1 (mutant) 
**[[2qtc]] - EcPDH E1 (mutant) + phosphonolactylthiamin diphosphate 
**[[1rp7]] - EcPDH E1 + inhibitor 
**[[4qoy]] - EcPDH E1 + PDH E2 

*Pyruvate dehydrogenase E2 see [[Dihydrolipoyl transacetylase]] and [[Dihydrolipoamide acetyltransferase]]; Domains – peripheral-subunit binding (PSB) 118-170; lipoyl 179-282; catalytic 395-697

**[[3b8k]], [[6ct0]], [[8piu]] – hPDH E2 – Cryo EM 
**[[7uom]] – hPDH E2 catalytic domain – Cryo EM 
**[[8x03]] – PDH E2 – bovine - Cryo EM 
**[[8x03]], [[9j1w]] – PDH E2 – pig - Cryo EM 
**[[7bgj]], [[7ott]], [[7q5r]] – PDH E2 – ''Thermochaetoides thermophila'' – Cryo EM 
**[[7b9k]], [[8orb]] – EcPDH E2 catalytic domain – Cryo EM 
**[[4n72]], [[8osy]] – EcPDH E2 catalytic domain 
**[[1fyc]], [[1qjo]], [[2k7v]] – EcPDH E2 lipoyl domain - NMR 
**[[8oqj]] - EcPDH E2 PSB 
**[[1w4i]], [[1w4j]], [[1w4k]] - PaPDH E2 PSB - NMR 
**[[1eaa]], [[1eab]], [[1eac]], [[1ead]], [[1eae]], [[1eaf]] – AvPDH E2 catalytic domain – Azotobacter vinelandii 
**[[1iyu]], [[1iyv]] – AvPDH E2 1-79 – NMR 
**[[6zzi]], [[6zzm]] – CmPDH E2 catalytic domain – Corynebacterium mustelae 
**[[6zzj]] – CmPDH E2 catalytic domain + acetylCoA 
**[[6zzl]] – CgPDH E2 catalytic domain - Corynebacterium glutamicum 
**[[6zzk]] – CgPDH E2 catalytic domain + acetylCoA + dihydropolyamide 
**[[9y6t]], [[9y72]] – MtPDH E2 catalytic domain – Mycobacterium tuberculosis – Cryo EM 
**[[9y7v]] – MtPDH E2 catalytic domain + acetylCoA – Cryo EM 
**[[9ukz]] - BsPDH E2 catalytic domain – ''Bacillus stearothermophilus'' – Cryo EM 
**[[1w3d]], [[2pdd]], [[2pde]] - BsPDH E2 PSB - NMR 
**[[1lab]], [[1lac]] – BsPDH E2 lipoyl domain - NMR 

*Pyruvate dehydrogenase E1+E2

**[[1w85]], [[1w88]] - BsPDH E1 α + β subunits + PDH E2 peripheral-subunit binding domain 
**[[3duf]], [[3dv0]] - BsPDH E1 α + β subunits + PDH E2 
**[[3dva]] - BsPDH E1 α (mutant) + β subunits + PDH E2 
**[[9h1n]] - EcPDH E1 2-50 + PDH E2 315-380 

*Pyruvate dehydrogenase E3 or dihydrolipoyl dehydrogenase

**[[6h60]] – hPDH protein X – Cryo EM 
**[[1zy8]] – hPDH protein X + dihydrolipoyl dehydrogenase 
**[[2f5z]] - hPDH protein X (mutant) + dihydrolipoyl dehydrogenase 
**[[2f60]] - hPDH protein X (mutant) 
**[[2dnc]], [[2dne]] - hPDH protein X N terminal - NMR 
**[[2g25]] - hPDH protein X + phosphonolactylthiamin diphosphate 
**[[2g28]] - hPDH protein X (mutant) + phosphonolactylthiamin diphosphate 
**[[2eq8]] – TtPDH E3 – ''Thermus thermophilus'' 
**[[4jdr]], [[4jq9]] – EcPDH E3 
**[[1gjx]] – PDH E3 lipoyl domain – ''Neisseria meningitis'' – NMR 
**[[6zlm]], [[6zlo]], [[7r5m]], [[8ohs]] – NcPDH protein X + E2 – ''Neurospora crassa'' - Cryo EM 

*Pyruvate dehydrogenase E2+E3

**[[9h2i]] - EcPDH E2 catalytic domain + PDH E3 
}}

[[Category:Topic Page]]

Pyruvate dehydrogenase

2026-08-27T07:56:56Z

Michal Harel:

<StructureSection load='1l8a' size='350' side='right' caption='E. coli pyruvate dehydrogenase dimer complex with thiamine diphosphate and Mg+2 ion (green) (PDB code [[1l8a]]).' scene=''>
==Function==

'''Pyruvate dehydrogenase''' (E1) is one of three main components of the multienzyme complex pyruvate dehydrogenase. It accompanies '''dihydrolipoyl transacetylase''' or '''dihydrolipoamide acetyltransferase''' (E2) and '''dihydrolipoyl dehydrogenase''' (E3) in comprising this multienzyme complex. The ''E. coli'' enzyme complex has a weight of approximately 4600-kD and a diameter of about 300 angstroms. The core of the particle is made of 24 E2 proteins arranged in a cube, which is surrounded by 24 E1 proteins and 12 E3 proteins. Together, these enzymes are responsible for synthesizing acetyl-CoA from pyruvate just prior to entrance into the citric acid cycle. Therefore, pyruvate dehydrogenase contributes to linking the glycolysis metabolic pathway to the citric acid pathway. For more details on E3 see [[Dihydrolipoamide dehydrogenase]].

See also [[Pyruvate Dehydrogenase (Hebrew)]].

==Structure==
Pyruvate dehydrogenase (E1) falls within the class of alpha and beta proteins<ref>Protein: Pyruvate dehydrogenase E1-beta, PdhB, C-terminal domain from Bacillus stearothermophilus. (2009). Retrieved from http://scop.mrc-lmb.cam.ac.uk</ref>, containing <scene name='Kenny_Coggins_Sandbox_1/Secondary_structure/1'>mixed alpha helices and beta sheets</scene>. It is a multimeric protein. Mammalian E1s, including human E1, are heterotetrameric, composed of two α- and two β- subunits<ref>Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS (June 2003). "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase". J. Biol. Chem. 278 (23): 21240–6</ref>. E1 from E. coli is, however, a homodimer with a molecular weight of 99474 containing α/β folds. It has two catalytic sites located at the interface between subunits. Each polypeptide chain consists of 886 residues<ref name="PMID">PMID:11955070</ref>. The structure shown is the E. coli E1 pyruvate dehydrogenase component, PDB code
[[1l8a]]<ref>Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/</ref>.

==Reactions and Mecahanism==
The multienzyme complex together catalyzes five distinct reactions in the conversion of pyruvate to acetyl-CoA. The overall result is described by the following reaction:

Pyruvate + CoA + NAD+ ==> Acetyl-CoA + CO2 + NADH

However, pyruvate dehydrogenase (E1) is responsible for only the first two of the five reactions. The first of these is the decarboxylation of pyruvate and coupling of thiamine pyrophosphate (TPP) to form hydroxyethyl-TPP.

Pyruvate + TPP ==> Hydroxyethyl-TPP + CO2

The enzyme requires <scene name='Kenny_Coggins_Sandbox_1/Thdp/5'>TPP and Mg2+</scene> as cofactors for catalysis. [[Image:Thiamine pyrophosphate.png|thumb|left|alt=Thiamine pyrophosphate.|Thiamine pyrophosphate (TPP) E1 cofactor.]]
{{Clear}}
In this reaction, the ylide form of TPP attacks the electrophilic carbonyl group of pyruvate. This reflects the ability of TPP’s thiazolium ring, which primarily interacts with <scene name='Kenny_Coggins_Sandbox_1/Ile569_asp521/5'>Ile569 and Asp521</scene>, to add to carbonyl groups. Decarboxylation of the resulting alkoxide yields an enol complex. This enol resonates to form the ylide form of hydroxyethyl-TPP<ref name="book">Voet, D., Voet, J.G., and Pratt, C.W. (2008). Fundamentals of biochemistry. Hoboken, NJ: John Wiley and Sons, Inc.</ref>. During this reaction, the catalytic Mg2+ ion coordinates octahedrally with three protein ligands: <scene name='Kenny_Coggins_Sandbox_1/Asp230_and_asn260/2'>Asp230 and Asn 260</scene>, which bind TPP, and <scene name='Kenny_Coggins_Sandbox_1/Glu262/2'>Gln262</scene><ref name="PMID" />.

The second E1-catalyzed reaction is the transfer of the hydroxyethyl group to the lipoamide group of the next enzyme, dihydrolipoyltransacetylase (E2). The E2 lipoamide group consisting of lipoic acid linked to the amide group of a Lys residue. Lipoic acid contains a reactive cyclic disulfide that is reversibly reduced to give dihydrolipoamide. The ylide form of the hydroxyethyl group of the hydroxyethyl-TPP complex attacks this disulfide bond. TPP is then eliminated as it detaches with E1 and subsequently binds to the next pyruvate molecule<ref name="book" />.

E1-Hydroxyethyl-TPP + E2-Lipoamide ==> E1-TPP + Acetyl-dihydrolipoamide-E2

The overall mechanism is shown as following:

[[Image:PyruvateDehydrgenaseMech.gif]]

==Regulation==
Pyruvate dehydrogenase plays a key role in the regulation of the Krebs cycle. The reactions catalyzed by the pyruvate dehydrogenase complex constitute the only biological pathway for acetyl-CoA synthesis from pyruvate. It is thus crucial that these reactions be precisely controlled.

One method of regulation is product inhibition by NADH and acetyl-CoA. NADH is a product of reactions catalyzed by dihydrolipoyl dehydrogenase (E3), while acetyl CoA is a product of the aforementioned dihydrolipoyl transacetylase (E2). Both compounds compete for active sites on their respective enzymes. NADH competes with NAD+ for E3 active site, while acetyl-CoA competes with CoA for E2 active site. High NADH levels keep E3 in its reduced form, thus the E2 lipoamide group stays in its reduced state. This in turn prevents E1 from transferring the hydroxyethyl group to E2. Consequently, E1 activity is reduced. Similarly, Acetyl CoA reduces E1 activity by occupying binding sites so less pyruvate binds to E1. Thus, high relative NADH and Acetyl-CoA concentrations regulate E1 activity through product inhibition.

These two compounds also activate the pyruvate dehydrogenase kinase associated with the enzyme complex<ref name="book" />. This results in phosphorylation of three different E1 serine residues (Ser 203, Ser 264, Ser 271) in human E1 and enzyme inactivation<ref>PMID:11092882</ref>. Enzyme regulation through phosphorylation by pyruvate dehydrogenase kinase and dephosphorylation pyruvate dehydrogenase phosphatase has been implicated as a target for treating cancer, heart ischemia, and diabetes<ref>PMID:17310282</ref>.

[[Image:400px-1400x1048_pdh_regulation.png]]

==Kinetics==
E. coli pyruvate dehydrogenase binding constant and maximum velocity values have been reported as Km = 0.3 mM and Vmax = 5,500 kat/mol (37 degrees C, pH = 7.6, 5 microM pyruvate, and 3 mg/L protein). The multienzyme complex exhibits postive cooperative binding (Hill constant = 1.9)<ref>Bisswanger, H. Substrate specificity of the pyruvate dehydrogenase complex from escherichia coli. J Biol Chem. 1981. Jan 25;256(2):815-822.</ref>.

==Medical Implications==
Pyruvate dehydrogenase is an autoantigen recognized in primary biliary cirrhosis. These antibodies appear to recognize oxidized protein that has resulted from inflammatory immune responses. Some of these inflammatory responses are explained by gluten sensitivity<ref> Leung PS, Rossaro L, Davis PA, et al. (2007). "Antimitochondrial antibodies in acute liver failure: Implications for primary biliary cirrhosis". Hepatology 46 (5): 1436</ref>. Other mitochondrial autoantigens include oxoglutarate dehydrogenase and branched-chain alpha-keto acid dehydrogenase complex, which are antigens recognized by anti-mitochondrial antibodies.

Pyruvate dehydrogenase (PDH) deficiency is a congenital degenerative metabolic disease resulting from a mutation of the pyruvate dehydrogenase complex (PDC) located on the X chromosome. Although defects have been identified in all 3 enzymes of the complex, the E1-α subunit is predominantly the culprit. Malfunction of the citric acid cycle due to PDH deficiency deprives the body of energy and leads to an abnormal buildup of lactate. PDH deficiency is a common cause of lactic acidosis in newborns and often presents with severe lethargy, poor feeding, tachypnea, and cases of death have occurred<ref>Frye, Richard E., and Paul J. Benke. "Pyruvate Dehydrogenase Complex Deficiency." EMedicine. 11 Dec. 2007. WebMD. 14 Dec. 2008 </ref>.

==3D structures of pyruvate dehydrogenase==
[[Pyruvate dehydrogenase 3D structures]]

</StructureSection>

==References==
<references/>
[[Category:Topic Page]]

Pyruvate dehydrogenase

2026-08-27T07:54:07Z

Michal Harel:

<StructureSection load='1l8a' size='350' side='right' caption='E. coli pyruvate dehydrogenase dimer complex with thiamine diphosphate and Mg+2 ion (green) (PDB code [[1l8a]]).' scene=''>
==Function==

'''Pyruvate dehydrogenase''' (E1) is one of three main components of the multienzyme complex pyruvate dehydrogenase. It accompanies '''dihydrolipoyl transacetylase''' (E2) and '''dihydrolipoyl dehydrogenase''' (E3) in comprising this multienzyme complex. The ''E. coli'' enzyme complex has a weight of approximately 4600-kD and a diameter of about 300 angstroms. The core of the particle is made of 24 E2 proteins arranged in a cube, which is surrounded by 24 E1 proteins and 12 E3 proteins. Together, these enzymes are responsible for synthesizing acetyl-CoA from pyruvate just prior to entrance into the citric acid cycle. Therefore, pyruvate dehydrogenase contributes to linking the glycolysis metabolic pathway to the citric acid pathway. For more details on E3 see [[Dihydrolipoamide dehydrogenase]].

See also [[Pyruvate Dehydrogenase (Hebrew)]].

==Structure==
Pyruvate dehydrogenase (E1) falls within the class of alpha and beta proteins<ref>Protein: Pyruvate dehydrogenase E1-beta, PdhB, C-terminal domain from Bacillus stearothermophilus. (2009). Retrieved from http://scop.mrc-lmb.cam.ac.uk</ref>, containing <scene name='Kenny_Coggins_Sandbox_1/Secondary_structure/1'>mixed alpha helices and beta sheets</scene>. It is a multimeric protein. Mammalian E1s, including human E1, are heterotetrameric, composed of two α- and two β- subunits<ref>Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS (June 2003). "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase". J. Biol. Chem. 278 (23): 21240–6</ref>. E1 from E. coli is, however, a homodimer with a molecular weight of 99474 containing α/β folds. It has two catalytic sites located at the interface between subunits. Each polypeptide chain consists of 886 residues<ref name="PMID">PMID:11955070</ref>. The structure shown is the E. coli E1 pyruvate dehydrogenase component, PDB code
[[1l8a]]<ref>Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/</ref>.

==Reactions and Mecahanism==
The multienzyme complex together catalyzes five distinct reactions in the conversion of pyruvate to acetyl-CoA. The overall result is described by the following reaction:

Pyruvate + CoA + NAD+ ==> Acetyl-CoA + CO2 + NADH

However, pyruvate dehydrogenase (E1) is responsible for only the first two of the five reactions. The first of these is the decarboxylation of pyruvate and coupling of thiamine pyrophosphate (TPP) to form hydroxyethyl-TPP.

Pyruvate + TPP ==> Hydroxyethyl-TPP + CO2

The enzyme requires <scene name='Kenny_Coggins_Sandbox_1/Thdp/5'>TPP and Mg2+</scene> as cofactors for catalysis. [[Image:Thiamine pyrophosphate.png|thumb|left|alt=Thiamine pyrophosphate.|Thiamine pyrophosphate (TPP) E1 cofactor.]]
{{Clear}}
In this reaction, the ylide form of TPP attacks the electrophilic carbonyl group of pyruvate. This reflects the ability of TPP’s thiazolium ring, which primarily interacts with <scene name='Kenny_Coggins_Sandbox_1/Ile569_asp521/5'>Ile569 and Asp521</scene>, to add to carbonyl groups. Decarboxylation of the resulting alkoxide yields an enol complex. This enol resonates to form the ylide form of hydroxyethyl-TPP<ref name="book">Voet, D., Voet, J.G., and Pratt, C.W. (2008). Fundamentals of biochemistry. Hoboken, NJ: John Wiley and Sons, Inc.</ref>. During this reaction, the catalytic Mg2+ ion coordinates octahedrally with three protein ligands: <scene name='Kenny_Coggins_Sandbox_1/Asp230_and_asn260/2'>Asp230 and Asn 260</scene>, which bind TPP, and <scene name='Kenny_Coggins_Sandbox_1/Glu262/2'>Gln262</scene><ref name="PMID" />.

The second E1-catalyzed reaction is the transfer of the hydroxyethyl group to the lipoamide group of the next enzyme, dihydrolipoyltransacetylase (E2). The E2 lipoamide group consisting of lipoic acid linked to the amide group of a Lys residue. Lipoic acid contains a reactive cyclic disulfide that is reversibly reduced to give dihydrolipoamide. The ylide form of the hydroxyethyl group of the hydroxyethyl-TPP complex attacks this disulfide bond. TPP is then eliminated as it detaches with E1 and subsequently binds to the next pyruvate molecule<ref name="book" />.

E1-Hydroxyethyl-TPP + E2-Lipoamide ==> E1-TPP + Acetyl-dihydrolipoamide-E2

The overall mechanism is shown as following:

[[Image:PyruvateDehydrgenaseMech.gif]]

==Regulation==
Pyruvate dehydrogenase plays a key role in the regulation of the Krebs cycle. The reactions catalyzed by the pyruvate dehydrogenase complex constitute the only biological pathway for acetyl-CoA synthesis from pyruvate. It is thus crucial that these reactions be precisely controlled.

One method of regulation is product inhibition by NADH and acetyl-CoA. NADH is a product of reactions catalyzed by dihydrolipoyl dehydrogenase (E3), while acetyl CoA is a product of the aforementioned dihydrolipoyl transacetylase (E2). Both compounds compete for active sites on their respective enzymes. NADH competes with NAD+ for E3 active site, while acetyl-CoA competes with CoA for E2 active site. High NADH levels keep E3 in its reduced form, thus the E2 lipoamide group stays in its reduced state. This in turn prevents E1 from transferring the hydroxyethyl group to E2. Consequently, E1 activity is reduced. Similarly, Acetyl CoA reduces E1 activity by occupying binding sites so less pyruvate binds to E1. Thus, high relative NADH and Acetyl-CoA concentrations regulate E1 activity through product inhibition.

These two compounds also activate the pyruvate dehydrogenase kinase associated with the enzyme complex<ref name="book" />. This results in phosphorylation of three different E1 serine residues (Ser 203, Ser 264, Ser 271) in human E1 and enzyme inactivation<ref>PMID:11092882</ref>. Enzyme regulation through phosphorylation by pyruvate dehydrogenase kinase and dephosphorylation pyruvate dehydrogenase phosphatase has been implicated as a target for treating cancer, heart ischemia, and diabetes<ref>PMID:17310282</ref>.

[[Image:400px-1400x1048_pdh_regulation.png]]

==Kinetics==
E. coli pyruvate dehydrogenase binding constant and maximum velocity values have been reported as Km = 0.3 mM and Vmax = 5,500 kat/mol (37 degrees C, pH = 7.6, 5 microM pyruvate, and 3 mg/L protein). The multienzyme complex exhibits postive cooperative binding (Hill constant = 1.9)<ref>Bisswanger, H. Substrate specificity of the pyruvate dehydrogenase complex from escherichia coli. J Biol Chem. 1981. Jan 25;256(2):815-822.</ref>.

==Medical Implications==
Pyruvate dehydrogenase is an autoantigen recognized in primary biliary cirrhosis. These antibodies appear to recognize oxidized protein that has resulted from inflammatory immune responses. Some of these inflammatory responses are explained by gluten sensitivity<ref> Leung PS, Rossaro L, Davis PA, et al. (2007). "Antimitochondrial antibodies in acute liver failure: Implications for primary biliary cirrhosis". Hepatology 46 (5): 1436</ref>. Other mitochondrial autoantigens include oxoglutarate dehydrogenase and branched-chain alpha-keto acid dehydrogenase complex, which are antigens recognized by anti-mitochondrial antibodies.

Pyruvate dehydrogenase (PDH) deficiency is a congenital degenerative metabolic disease resulting from a mutation of the pyruvate dehydrogenase complex (PDC) located on the X chromosome. Although defects have been identified in all 3 enzymes of the complex, the E1-α subunit is predominantly the culprit. Malfunction of the citric acid cycle due to PDH deficiency deprives the body of energy and leads to an abnormal buildup of lactate. PDH deficiency is a common cause of lactic acidosis in newborns and often presents with severe lethargy, poor feeding, tachypnea, and cases of death have occurred<ref>Frye, Richard E., and Paul J. Benke. "Pyruvate Dehydrogenase Complex Deficiency." EMedicine. 11 Dec. 2007. WebMD. 14 Dec. 2008 </ref>.

==3D structures of pyruvate dehydrogenase==
[[Pyruvate dehydrogenase 3D structures]]

</StructureSection>

==References==
<references/>
[[Category:Topic Page]]

Pyruvate decarboxylase

2026-08-25T10:15:46Z

Michal Harel:

<StructureSection load='1zpd' size='450' side='right' scene='' caption='Pyruvate decarboxylate complex with phosphono ester, citrate and Mg+2 ion (green) (PDB code [[1zpd]])'>
==The Enzyme Pyruvate Decarboxylase==

[[Image:Pyruvate decarb 1.jpg|left|450px|thumb]]

'''Image 1: Reaction catalyzed by pyruvate decarboxylase:
pyruvate + thiamine pyrophasphate (TPP) → hydroxyethyl-TPP + CO2.'''

==Importance in Anaerobic Metabolism==

Pyruvate, NADH, and ATP are the products of glycolysis. Under anaerobic conditions, pyruvate undergoes fermentation to oxidize NADH to
NAD+, so glycolysis can continue. In alcoholic fermentation, which occurs in some yeast, this is a two-step process. The first involves the Enzyme pyruvate decarboxylase (PDC). The pyruvate is decarboxylated to an acetaldehyde. This acetaldehyde then undergoes a reaction catalyzed by alcohol dehydrogenase to produce ethanol; this is the step in which the NAD+ is restored <ref>Garrett, R.H., & Grisham, C.M. (2007). Biochemistry. Belmont, CA: Thompson.</ref>.

==Structure==
Pyruvate decarboxylase is a homotetramer. Each identical subunit consists of approximately alternating α-helices and β-sheets, and 2 domains exist within each 60kDa <scene name='Ken_Engle_SANDBOX/Subunit/7'>subunit</scene>. This means its SCOP category is alpha and beta protein <ref>PMID:9685367</ref>. Being a homotetramer, pyruvate PDC has 4 identical <scene name='Ken_Engle_SANDBOX/Active_site/3'>active sites</scene> that are green surrounding the ligands when the previous link is selected.

==Active Site==

The <scene name='40/401493/Active_site/1'>active site</scene> of PDC consists of Glu 477, Asp28, His114, and His 115 as well as the thiamine diphosphate cofactor. Hydrogen bonding occurs between the substrate and Asp28, His114, and Thr73. In the catalytic step of the reaction mechanism, <scene name='Ken_Engle_SANDBOX/Glu_473/2'>Glu 473</scene>, shown in red, donates a proton to the pyruvate. The scene shows the close proximity of this residue to the pyruvate. The negative charge of the Glu residue following the protonation of the substrate leads to the destabilization of the pyruvate carboxylate group. Next the carboxyl group leaves, using thyiamine diphosphate as an electron sink (described below). Following decarboxylation in the final step of the mechanism, release of acetaldehyde, a proton is transferred to the Glu477 residue from a cofactor. After the protonation in a concerted step, a water molecule donates a proton to the substrate while receiving a proton from Glu477. As the proton is taken from the substrate, the electrons move to form a carbonyl, which leads to the release of the acetaldehyde.

==Regulation==

PDC is regulated by substrate activation. This means that if substrate is not present in the pathway, the protein will be "off." The residue that is bound to start a cascade of events resulting in the activation of the enzyme is <scene name='Ken_Engle_SANDBOX/Regulation_site/3'>C 221</scene><ref>PMID: 11412092 </ref> which is highlighted in pink in the scene. This process allows the enzyme to be on when its function is necessary and off when it would not be catalyzing the reaction even if it were on.

==ThDP an Important Cofactor==

Thiamine diphosphate (ThDP) is an important cofactor in alpha decarboxylation reactions. The structure of ThDP is <scene name='40/401493/Bent_tpp/1'>bent</scene> when bound to the protein. This kink brings the 4'N of ThDP in close enough proximity to C2 to <scene name='40/401493/Deprotonation/2'>deprotonate</scene> it, forming a reactive ylid <ref>PMID:PMID: 8974393</ref>. Glutamic acid 51 on the other side of ThDP forms a <scene name='40/401493/Glu51_h_bond_to_thdp/1'>hydrogen bond</scene> with ThDP to increase the basicity of 4'N. In the decarboxylation reaction, <scene name='40/401493/Tpp_c2/1'>C2</scene> of ThDP is deprotonated, and attacks C2 of the pyruvate (this structure has pyruvamide instead of pyruvate), resulting in a <scene name='40/401493/Tpp_c2_to_c2/1'>covalent bond</scene> between ThDP and the pyruvate. This allows the ThDP to act as an electron sink for the decarboxylation reaction.
</StructureSection>
__NOTOC__

==3D structures of pyruvate decarboxylase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyruvate decarboxylase

**[[1zpd]], [[2wva]], [[2wvg]], [[2wvh]] - ZmPyD – ''Zymomonas mobilis'' 
**[[2vk4]], [[6efg]] – KlPyD – ''Kluveromyces lactis'' 
**[[2vbi]] – PyD – ''Acetobacter pasteurianus'' 
**[[3mve]] - VvPyD - ''Vibrio vulnificus'' 
**[[5euj]] - PyD - ''Zymobacter palmae'' 
**[[8hp2]] - CtPyD – ''Candida tropicalis'' 

*Pyruvate decarboxylase complex

**[[1pvd]], [[1pyd]], [[1qpb]] - yPyD + ThDP - yeast 
**[[2w93]] - yPyD (mutant) + ThDP 
**[[2vk1]] - yPyD (mutant) + pyruvic acid + ThDP 
**[[2vk8]] - yPyD (mutant) + hydroxypropanoic acid + ThDP 
**[[2vjy]] – KlPyD + substrate analog 
**[[6efh]] - KlPyD + ThDP 
**[[4cok]] - PyD + ThDP – ''Glucanacetobacter diazotrophicus'' 
**[[3our]] - VvPyD + EIIA 
**[[5npu]] - PyD + TPP - synthetic 
**[[3oe1]], [[4zp1]], [[5tma]] – ZmPyD (mutant) + ThDP derivative 
**[[9s7j]] - PyD + ThDP – ''Neoasaia chiangmaiensis'' – Cryo EM 
**[[8hp4]] - CtPyD + ThDP 
}}
==Additional Resources==
For additional information, see: [[Carbohydrate Metabolism]]
 

==References==

<references />

[[Category:Topic Page]]

Aminoacyl tRNA synthetase 3D structures

2026-08-25T09:57:03Z

Michal Harel:

== 3D Structures of [[Aminoacyl tRNA Synthetase]] ==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}

{{#tree:id=OrganizedByTopic|openlevels=0|
*Class I aaRS
*'''Arg-RS'''
**[[4zaj]] - hArgRS – human 
**[[4q2y]] – hArgRS (mutant) 
**[[1bs2]] – yArgRS - yeast 
**[[3gdz]] – KpArgRS residues 1-106 – ''Klebsiella pneumoniae'' 
**[[1iq0]] – TtArgRS - ''Thermus thermophilus'' 
*''Arg-RS + small substrates or analogs''
**[[4q2t]] – hArgRS (mutant) + Arg 
**[[4q2x]] – hArgRS (mutant) + canavanine 
**[[6ao8]] - NgArgRS + Arg – ''Neisseria gonorrhoeae'' 
**[[5yym]], [[4oby]] - EcArgRS + Arg – ''Escherichia coli'' 
* ''Arg-RS + tRNA''
**[[1f7v]] - yArgRS + Arg-tRNA 
**[[2zuf]] - PhArgRS + tRNA-Arg - ''Pyrococcus horikoshii'' 
**[[5yyn]], [[5b63]] - EcArgRS + Arg-tRNA 
* ''Arg-RS ternary complex''
**[[4z3z]] - hArgRS + GlnRS + AIMP1 
**[[1f7u]] – yArgRS + Arg-tRNA + Arg 
**[[2zue]] – PhArgRS + tRNA-Arg + ATP analog 
*'''Cys-RS'''
**[[1li5]] - EcCysRS 
**[[1li7]] - EcCysRS + Cys 
**[[1u0b]] – EcCysRS + Cys-tRNA 
**[[3tqo]] – CysRS – ''Coxiella burnetii'' 
**[[3sp1]] - BbCysRS – ''Borrelia burgdorferi'' 
**[[3c8z]] – MsCysRS + Cys-SA - ''Mycobacterium smegmatis'' 
**[[6ujd]] - ElCysRS (mutant) – ''Elizabethkingia'' 
*'''Gln-RS'''
**[[4ye6]] – hGlnRS 
**[[4ye8]], [[4ye9]] – hGlnRS (mutant) 
**[[4h3s]] – yGlnRS 
**[[3tl4]] – yGlnRS tRNA-binding domain 
**[[1nyl]] – EcGlnRS 
**[[5zdo]] – TtGlnRS 
**[[5zdk]], [[5zdl]] – TtGlnRS + ATP 
**[[2gls]], [[1lgr]] – StGlnRS – ''Salmonella typhimurium'' 
**[[5bnz]] – PaGlnRS – ''Pseudomonas aeruginosa'' 
**[[4p2b]] – TgGlnRS catalytic domain – ''Toxoplasma gondii'' 
**[[2lgs]] – StGlnRS + Glu 
**[[1gtr]], [[1gts]], [[1gsg]] - EcGlnRS + Gln-tRNA 
* ''Gln-RS ternary complex''
**[[1euq]], [[1euy]] – EcGlnRS + Gln-tRNA + Gln-SA 
**[[1exd]] - EcGlnRS + Gln-tRNA (mutant) + AMP 
**[[4jxx]], [[4jxz]], [[4jyz]] - EcGlnRS + Gln-tRNA + ATP 
**[[1qtq]] - EcGlnRS + Gln-tRNA + Gln analog 
*'''Glu-RS'''
**[[2hra]] – yGluRS N-terminal 
**[[1gln]] – TtGluRS 
**[[2o5r]] - TmGluRS 
**[[3aii]] – GluRS – ''Methanothermobacter thermautotrophicus'' 
**[[2ja2]], [[3pny]] – MtGluRS – ''Mycobacterium tuberculosis'' 
**[[3pnv]] - MtGluRS (mutant) 
**[[4a91]] – EcGluRS 
**[[2hz7]] – DrGluRS – ''Deinococcus radiodurans'' 
**[[6b1p]] - HpGluRS – ''Helicobacter pylori'' 
**[[6b1z]] - EaGluRS – ''Elizabethkingia anophelis'' 
**[[5tgt]] – PaGluRS 
**[[5h4v]] – GluRS – ''Xanthomonas oryzae'' 
**[[7k86]] – SmGluRS – ''Stenotrophomonas maltophilia'' 
* ''Glu-RS + small substrates or analogs''
**[[3afh]] - TmGluRS + Glu-AMP analog 
**[[2rd2]], [[2re8]] – EcGluRS (mutant) + Glu-SA 
**[[2cuz]] – TtGluRS + Glu 
**[[1j09]] - TtGluRS + Glu + ATP 
**[[1n75]] - TtGluRS + ATP 
**[[2cfo]] - GluRS residues 2-485 + Glu – ''Synechococcus elongatus'' 
**[[6brl]] - GluRS + Glu - ''Elizabethkingia meningoseptica'' 
**[[4grl]] - BbGluRS + Glu 
**[[4g6z]] - BtGluRS + Glu – ''Burkholderia thailandensis'' 
* ''Glu-RS + tRNA''
**[[1zjw]] – EcGluRS + Glu-tRNA 
**[[1g59]] – TtGluRS + Glu-tRNA 
* ''Glu-RS ternary complex''
**[[5bmu]] – hGluRS GST-like domain + EPRS-AIMP3 
**[[2hrk]], [[2hsm]] - yGluRS N-terminal + GU4 nucleic-binding protein 1 
**[[3akz]], [[3al0]] – TmGluRS + tRNA + Glu-AMP analog – ''Thermotoga maritima'' 
**[[1o0b]], [[1o0c]] - EcGluRS + Glu-tRNA + Glu + AMP 
**[[2cv0]], [[1n77]] - TtGluRS + Glu + Glu-tRNA 
**[[1n78]] - TtGluRS + Glu-ol + Glu-tRNA 
**[[2cv1]] - TtGluRS + Glu-ol + ATP + Glu-tRNA 
**[[2cv2]] - TtGluRS + Glu-SA + Glu-tRNA 
*'''Ile-RS'''
**[[1ile]] - TtIleRS 
**[[1wny]], [[1udz]] – TtIleRS editing domain 201-381 
* ''Ile-RS + small substrates or analogs''
**[[1ue0]] - TtIleRS editing domain + Val 
**[[1wnz]] - TtIleS editing domain + Val-adenylate 
**[[1wk8]] - TtIleRS editing domain + Val-SA 
**[[1jzq]] – TtIleS + Ile-adenylate analog 
**[[1jzs]] – TtIleS + antibiotic 
* ''Ile-RS ternary complex''
**[[1ffy]], [[1qu2]], [[1qu3]] - SaIleRS + Ile-tRNA + antibiotic - ''Staphylococcus aureus'' 
**[[6ldk]] - CaIleRS + AMP + Ile – ''Candida albicans'' 
*'''Leu-RS'''; Domains – editing 260-530;
**[[2wfd]] – hLeuRS editing domain 260-509 
**[[3o0a]], [[3pz0]] – AaLeuRS editing domain – ''Aquifex aeolicus'' 
**[[3pz5]] – AaLeuRS editing domain (mutant) 
**[[2wfe]] - CaLeuRS editing domain – ''Candida albicans'' 
**[[5agh]] - CaLeuRS editing domain (mutant) 
**[[2ajg]] - EcLeuRS editing domain 228-413 
**[[1wkb]] – PhLeuRS residues 1-810 
**[[5fon]] - CmLeuRS editing domain – ''Cryptosporidium muris'' 
**[[5foc]] - PfLeuRS editing domain 
**[[5fod]] - PfLeuRS editing domain (mutant) 
**[[5fof]] - LeuRS editing domain – ''Plasmodium knowlesi'' 
**[[4k48]] - SpLeuRS editing domain (mutant) – ''Streptococcus pneumoniae'' 
**[[3pz6]] - LeuRS editing domain (mutant) – ''Giardia intestinalis'' 
**[[7nu4]] - NgLeuRS 
**[[7nty]], [[7nu1]], [[7nua]] - NgLeuRS (mutant) 
**[[7n11]] - MaLeuRS editing domain – ''Mycobacteroides abscessus'' 
* ''Leu-RS + small substrates or analogs''
**[[6kqy]] - hLeuRS + Leu 
**[[7d5c]] - yLeuRS + inhibitor 
**[[7nu5]] - NgLeuRS + Leu 
**[[6ykk]], [[6ykl]], [[6ykn]], [[6yko]], [[6ykq]], [[6yks]], [[6ykt]], [[6yku]], [[6ykv]], [[6kyw]], [[6ykx]], [[7a0p]], [[7ap2]] - NgLeuRS (mutant) + inhibitor 
**[[6q89]], [[6q8a]], [[6q8b]], [[6q8c]], [[7ntz]], [[7nu2]], [[7nub]] - NgLeuRS (mutant) + intermediate analog 
**[[7nu6]], [[7nu7]] - NgLeuRS + ATP 
**[[7nu9]] - NgLeuRS + ATP + leucinol 
**[[7nu3]], [[7nuc]] - NgLeuRS (mutant) + ATP + leucinol 
**[[7nu8]] - NgLeuRS + Leu-AMP 
**[[2wfg]] - CaLeuRS editing domain + benzoxaborole-AMP 
**[[1h3n]] - TtLeuRS + Leu-SA 
**[[1obc]], [[1obh]] – TtLeuRS + substrate analog 
**[[2ajh]], [[2aji]] - EcLeuRS editing domain + aa 
**[[4aq7]] - EcLeuRS editing domain + Leu-adenylate analog 
**[[4cqn]] - EcLeuRS editing domain + Ile-adenylate analog 
**[[5fog]] - CmLeuRS editing domain + norvaline 
**[[5fol]] - CmLeuRS editing domain + Ile 
**[[5fom]] - CmLeuRS editing domain + inhibitor 
**[[5agj]] - CaLeuRS editing domain + AMP derivative 
**[[5agi]] - CaLeuRS editing domain (mutant) + AMP derivative 
**[[5agr]], [[5ags]], [[5agt]] - MtLeuRS editing domain + inhibitor 
**[[7bzj]] - SpLeuRS + inhibitor 
**[[4k47]] - SpLeuRS editing domain (mutant) + benzoxaborole-AMP 
**[[3ziu]] - LeuRS editing domain + Leu-SA – ''Mycoplasma mobile'' 
**[[7n12]] - MaLeuRS editing domain + epetraborole-AMP 
* ''Leu-RS + tRNA''
**[[1wz2]] – PhLeuRS + Leu-tRNA 
**[[5ah5]] - LeuRS + Leu-tRNA – ''Agrobacterium radiobacter'' 
* ''Leu-RS ternary complex''
**[[6kie]], [[6kr7]] - hLeuRS + Leu-SA + Leu 
**[[6lpf]], [[6lr6]] - hLeuRS + Leu-SA + adenosine derivative 
**[[6kid]] - hLeuRS + ATP + Leu 
**[[4arc]] - EcLeuRS + Leu-tRNA + Leu 
**[[5omw]] - EcLeuRS + Leu-tRNA + Leu-adenylate analog 
**[[4ari]], [[4as1]], [[3zjt]], [[3zju]], [[3zjv]] - EcLeuRS + Leu-tRNA + benzoxaborole 
**[[3zgz]] - EcLeuRS + Leu-tRNA + inhibitor 
**[[5onh]] - EcLeuRS + Leu-tRNA + Leu-adenylate analog + norvaline 
**[[5on2]] - EcLeuRS (mutant) + Leu-tRNA + Leu-adenylate analog + norvaline 
**[[5on3]] - EcLeuRS (mutant) + Leu-tRNA + Leu-adenylate analog + Leu 
**[[2v0g]] - TtLeuRS + Leu-tRNA + benzoxaborole-AMP 
**[[2bte]], [[2byt]] - TtLeuRS + Leu-tRNA + Leu 
**[[2v0c]] – TtLeuRS + Leu-SA + benzoxaborole-AMP 
*'''Lys-RS'''
**[[3bju]] – hLysRS residues 70-579 
**[[6ilh]], [[7ea9]] - hLysRS (mutant) 
**[[7f6w]] – yLysRS 
**[[1irx]] – PhLysRS 
**[[1bbw]] – EcLysRS 
**[[5yzx]] - EcLysRS (mutant) 
**[[1krs]], [[1krt]] – EcLysRS anticodon-binding domain – NMR 
**[[3dsq]] – DhLysRS – ''Desulfitobacterium hafniense'' 
**[[4up8]] - EhLysRS – ''Entamoeba histolytica'' 
**[[4h02]] - PfLysRS – ''Plasmodium falciparum'' 
* ''Lys-RS binary complexes''
**[[6chd]] - hLysRS + Lys-adenylate derivative 
**[[4up7]] - EhLysRS + Lys-adenylate 
**[[4up9]] - EhLysRS + ATP 
**[[4upa]] - EhLysRS (mutant) + AMPPNP 
**[[3e9h]], 3e9i]] – BsLysRS + Lys-SA - ''Bacillus stearothermophilus'' 
**[[3a74]] - BsLysRS + diadenosine tetraphosphate 
**[[5zh2]], [[5zh3]], [[5zh4]], [[5zh5]], [[4pg3]], [[6hcv]] - PfLysRS + inhibitor 
**[[4ycv]] - PfLysRS + cladosporin 
**[[5vl1]] - MuLysRS + Lys – ''Mycobacterium ulcerans'' 
**[[5hgq]] - LysRS + cladosporin – eye worm 
**[[1bbu]], [[1e1o]], [[1lyl]] – EcLysRS + Lys 
**[[1e1t]] - EcLysRS + Lys-adenylate 
**[[6c86]] - CpLysRS + Lys-adenylate derivative - ''Cryptosporidium parvum'' 
**[[5eln]] - CpLysRS + Lys 
**[[4ex5]] - BtLysRS + Lys 
**[[6wbd]] - SmLysRS + Lys 
*''Lys-RS ternary complexes''
**[[6ild]], [[4dpg]] - hLysRS + P38 + AIMP2 
**[[4ycu]] - hLysRS + P38 + cladosporin 
**[[4ycw]] - hLysRS (mutant) + P38 + cladosporin 
**[[1e22]] - EcLysRS + Lys + AMPPCP 
**[[1e24]] - EcLysRS + Lys + ATP 
**[[6nrz]] - CtLysRS + Lys + adenosine – ''Chlamydia trachomatis'' 
**[[6ns0]], [[6o3f]] - CtLysRS + Lys + cladosporin 
**[[6bni]] - CpLysRS + Lys + adenine 
**[[5elo]] - CpLysRS + Lys + cladosporin 
**[[6aqg]] - MuLysRS + Lys + cladosporin 
**[[6agt]], [[6ka6]], [[6kab]], [[6kbf]], [[6kcn]], [[6kct]] - PfLysRS + Lys + cladosporin derivative 
**[[7bt5]] - PfLysRS + Lys + drug 
**[[6hcu]], [[6hcw]] - PfLysRS + Lys + inhibitor 
**[[6aqh]] - LysRS + Lys + cladosporin – ''Mycobacterium thermoresistibile'' 
*'''Met-RS'''
**[[5gl7]] – hMetRS residues 221-834 
**[[2djv]] – hMetRS WHEP-TRS domain 835-900 – NMR 
**[[1med]], [[1mea]] – EcMetRS Zinc-binding domain - NMR 
**[[1qqt]], [[3h9c]] - EcMetRS residues 2-552 
**[[3h97]], [[6spp]] – EcMetRS residues 2-548 (mutant) 
**[[1a8h]] – TtMetRS 
**[[2d54]], [[2d5b]] – TtMetRS (mutant) 
**[[1woy]] – TtMetRS residues 1-500 (mutant) 
**[[1pyb]] – AaMetRS subunit 
**[[1rqg]] – PabMetRS – ''Pyrococcus abyssi'' 
**[[1mkh]] – PabMetRS C-terminal 
**[[5xgq]] – MtMetRS 
**[[5h34]] – NeMetRS C-terminal – ''Nanoarchaeum equitans'' 
**[[2x1l]] - MsMetRS residues 2-515 
**[[7wpj]] – SaMetRS 
* ''Met-RS + small substrates or analogs''
**[[5goy]] – hMetRS residues 221-834 + Met 
**[[3kfl]] – LmMetRS residues 206-747+ Met-adenylate - ''Leishmania major'' 
**[[2x1m]] - MsMetRS residues 2-515 + Met 
**[[1p7p]], [[1pfu]], [[1pfv]], [[1pfw]] - EcMetRS residues 2-548 + Met 
**[[1pfy]] - EcMetRS residues 1-551 + Met-SA 
**[[1f4l]], [[6spo]] - EcMetRS residues 1-551 + Met 
**[[6spq]] - EcMetRS (mutant) + Met 
**[[6spn]] - EcMetRS + beta-Met 
**[[6spr]] - EcMetRS (mutant) + beta-Met 
**[[1pg0]] - EcMetRS residues 1-551 + Met-adenylate 
**[[1pg2]] - EcMetRS residues 1-551 + Met + adenine 
**[[3h99]] - EcMetRS residues 2-548 (mutant) + Met 
**[[3h9b]] - EcMetRS residues 2-548 (mutant) + azidonorleucine 
**[[4dlp]] - BmMetRS + SMet – ''Brucella melitensis'' 
**[[4py2]] – BmMetRS + inhibitor 
**[[6ax8]], [[5xet]] – MtMetRS + Met-adenylate 
**[[3vu8]] – TtMetRS + Met-adenylate analog 
**[[5urb]] - AbMetRS + Met – ''Acinetobacter baumannii'' 
**[[5k0s]], [[5k0t]] – MetRS + inhibitor – ''Brucella suis'' 
**[[4zt2]], [[4zt3]], [[4zt4]], [[4zt5]], [[4zt6]], [[4zt7]], [[4mvw]], [[4mvx]], [[4mvy]], [[4mw0]], [[4mw1]], [[4mw2]], [[4mw4]], [[4mw5]], [[4mw6]], [[4mw7]], [[4mw9]], [[4mwb]], [[4mwc]], [[4mwd]], [[4mwe]] - TbMetRS residues 237-773 (mutant) + inhibitor – ''Trypanosoma brucei'' 
**[[6cml]], [[6mes]] - TbMetRS residues 237-773 (mutant) + Met + inhibitor 
**[[4qrd]], [[4qre]] - SaMetRS + antibacterial 
**[[7wpi]], [[7wpn]] - SaMetRS + inhibitor 
**[[7wpk]] - SaMetRS + Met 
**[[7wpl]] - SaMetRS + ATP 
**[[7wpm]], [[7wpt]], [[7wpx]], [[7wq0]] - SaMetRS + inhibitor + ATP 
**[[7ulz]] - PaMetRS + Met 
* ''Met-RS + tRNA''
**[[2csx]] – AaMetRS + Met-tRNA 
**[[2ct8]] - AaMetRS + Met-tRNA + Met-SA 
**[[2dxi]] – TtMetRS + tRNA + ATP + Glu-ol 
* ''Met-RS + protein''
**[[4bl7]], [[4bvx]], [[4bvy]] - hMetRS N-terminal + elongation factor P18 
**[[2hsn]] - yMetRS N-terminal + GU4 nucleic-binding protein 1 N-terminal 
*'''Trp-RS'''
**[[1o5t]], [[1ulh]] – hTrpRS catalytic fragment 
**[[5uji]] – hTrpRS catalytic fragment (mutant) 
**[[3kt0]], [[2ip1]] – yTrpRS 
**[[1d2r]] - BsTrpRS 
**[[3prh]] – TrpRS (mutant) – ''Bacillus subtilis'' 
**[[3n9i]] – TrpRS – ''Yersinia pestis'' 
**[[3m5w]] – CjTrpRS – ''Campylobacter jejuni'' 
**[[3a04]] – ApTrpRS – ''Aeropyrum pernix'' 
**[[3hzr]] – EhTrpRS 
**[[3i05]] – TbTrpRS residues 3-389 
**[[3hv0]] – CpTrpRS residues 206-593 
**[[3foc]] – GlTrpRS – ''Giardia lamblia'' 
**[[2el7]] – TtTrpRS 
**[[2yy5]] – TrpRS – ''Mycoplasma pneumoniae'' 
**[[2g36]] – TmTrpRS 
**[[6mtk]] - EaTrpRS 
**[[5tev]] - NgTrpRS 
**[[4j76]] - PfTrpRS 
**[[7el8]] - MtTrpRS 
* ''Trp-RS + small substrates or analogs''
**[[5ujj]] – hTrpRS + Trp-AMP 
**[[2quh]] – hTrpRS + Trp 
**[[2qui]] - hTrpRS + Trp-amide + ATP 
**[[2quj]] - hTrpRS + Trp-adenylate 
**[[2quk]] – hTrpRS + ATP 
**[[3kt3]] – yTrpRS + Trp-adenylate 
**[[3kt6]], [[3kt8]] – yTrpRS + Trp 
**[[3a05]] – ApTrpRS + Trp 
**[[3jxe]] – PhTrpRS + Trp-adenylate 
**[[2ov4]] – BsTrpRS + adenosine tetraphosphate 
**[[1i6k]], [[1i6l]], [[1i6m]] – BsTrpRS + Trp-adenylate 
**[[1maw]], [[1m83]] - BsTrpRS + ATP 
**[[1mb2]] - BsTrpRS + Trp 
**[[7cms]] - BsTrpRS + antibiotic 
**[[1yid]], [[2a4m]] – DrTrpRS + ATP 
**[[1yi8]], [[1yia]]– DrTrpRS + Trp 
**[[1bks]] – StTrpRS + pyridoxal phosphate 
**[[6ncr]] - CtTrpRS + Trp 
**[[5tew]] - NgTrpRS + Trp 
**[[4j75]] - PfTrpRS + Trp-AMP 
**[[7elt]] - MtTrpRS + Trp-AMP 
**[[6dfu]] - TrpRS + Trp – ''Haemophilus influenzae'' 
*''Trp-RS ternary complex''
**[[5ekd]] – hTrpRS + ATP + antibiotic 
**[[5dk4]], [[7cki]] – BsTrpRS + ATP + antibiotic 
**[[7eer]] – BsTrpRS + ATP + inhibitor 
**[[3fhj]], [[3ghd]], [[3fi0]] – BsTrpRS + Trp + AMP + Pi 
**[[1mau]] – BsTrpRS + Trp + ATP 
**[[5v0i]] - EcTrpRS + Trp + AMP 
**[[7ens]] – MtTrpRS + ATP + antibiotic 
**[[7ent]], [[7ev2]], [[7ev3]] – MtTrpRS + ATP + inhibitor 
* ''Trp-RS + tRNA''
**[[2ake]], [[2dr2]] - hTrpRS + Trp-tRNA 
**[[2azx]] – hTrpRS (mutant) + tRNA 
*'''Tyr-RS'''
**[[1n3l]] - hTyrRS 
**[[5thh]], [[5thl]] - hTyrRS (mutant) 
**[[1ntg]] - hTyrRS C-terminal 
**[[1r6t]], [[1r6u]] – yTyrRS (mutant) 
**[[1tya]], [[1tyb]], [[1tyc]], [[1tyd]], [[2ts1]] – BsTyrRS 
**[[1jh3]] – BsTyrRS C-terminal – NMR 
**[[3qe4]], [[3d6u]], [[3d6v]], [[2pxh]], [[2hgz]], [[1u7d]], [[5n5v]], [[5nsf]], [[7c5c]], [[7ckh]] – MjTyrRS – ''Methanocaldococcus jannaschii'' 
**[[1u7x]], [[4hjr]], [[4hk4]], [[5u36]], [[5l7p]] - MjTyrRS (mutant) 
**[[2jan]] – MtTyrRS 
**[[1y42]], [[4ojm]] - NcTyrRS – ''Neurospora crassa'' 
**[[2cya]] – ApTyrRS 
**[[6n0w]] - EaTyrRS 
**[[6byq]] - HpTyrRS 
**[[6bqz]], [[6bqy]] - AbTyrRS 
**[[5ihx]] - AnTyrRS – ''Aspergillus nidulans'' 
**[[2ktl]] - AnTyrRS C-terminal - NMR 
**[[5ijx]] - TyrRS – ''Coccidiodides posadasii'' 
**[[7fg6]] - NeTyrRS 
* ''Tyr-RS + small substrates or analogs''
**[[1q11]] – hTyrRS residues 1-364 + Tyr-ol 
**[[2pid]] – hTyrRS residues 28-375 + Tyr-SA 
**[[4q93]] - hTyrRS + resveratrol 
**[[4qbt]] - hTyrRS + Tyr 
**[[3zxi]] - hTyrRS + Tyr-adenylate analog 
**[[7rou]] – hTyrRS + Tyr derivative 
**[[3ts1]] – BsTyrRS + Tyr-adenylate intermediate 
**[[4ts1]] – BsTyrRS + Tyr 
**[[3p0h]], [[3p0i]], [[3p0j]] – LmTyrRS + inhibitor 
**[[3n2y]] – MjTyrRS + tetrazolyl phenylalanine 
**[[2zp1]] – MjTyrRS (mutant) + Tyr 
**[[1zh0]] - MjTyrRS (mutant) + naphthyl-Ala 
**[[1zh6]], [[2ag6]], [[4pbr]], [[7ckg]] - MjTyrRS (mutant) + Phe derivative 
**[[4hjx]] - MjTyrRS (mutant) + di-fluoro-Tyr 
**[[4nx2]] - MjTyrRS (mutant) + di-chloro-Tyr 
**[[4hpw]] - MjTyrRS (mutant) + methyl-Tyr 
**[[5n5u]] - MjTyrRS + borono-Phe + AMP 
**[[2yxn]] – EcTyrRS residues 1-322 + azido-Tyr 
**[[1vbm]] – EcTyrRS + Tyr-SA 
**[[1vbn]] – EcTyrRS (mutant) + Tyr-SA 
**[[1x8x]] – EcTyrRS + Tyr 
**[[1wq3]], [[1wq4]] - EcTyrRS (mutant) + Tyr 
**[[6wn2]], [[6wrn]], [[6wrt]] - EcTyrRS (mutant) + Tyr derivative 
**[[4oud]] - EcTyrRS + bi-Phe 
**[[6i5y]] - EcTyrRS + Tyr-SA 
**[[6hb5]] - EcTyrRS + Tyr-SC 
**[[6hb6]], [[6hb7]] - EcTyrRS + Tyr-SU 
**[[7ap3]] - EcTyrRS + inhibitor 
**[[2j5b]] – TyrRS residues 2-346 + Tyr-ol – Acanthamoeba polyphaga minivirus 
**[[2cyb]] – AfTyrRS + Tyr - ''Archaeoglobus fulgidus'' 
**[[2cyc]] – PhTyrRS + Tyr 
**[[1h3f]]- TtTyrRS + Tyr-ol 
**[[1jii]], [[1jij]], [[1jil]], [[1jik]] – SaTyrRS + inhibitor 
**[[6otj]] – NgTyrRS + Tyr 
**[[7ror]] – PfTyrRS + Tyr-AMP 
**[[7ros]] – PfTyrRS + Tyr derivative 
**[[7rot]] – PfTyrRS (mutant) + Tyr derivative 
* ''Tyr-RS + tRNA''
**[[2dlc]] – yTyrRS + tRNA + Tyr-SA 
**[[1j1u]] – MjTyrRS + Tyr-tRNA 
**[[1h3e]] - TtTyrRS + Tyr-tRNA + Tyr-ol + ATP 
**[[2rkj]] – NcTyrRS + RNA 
**[[7sc6]], [[7scq]] – TyrRS + RNA – ''Phaseolus vulgaris'' 
*'''3-nitroTyr-RS'''
**[[4nd6]], [[4nd7]] - MjNTyrRS (mutant) 
**[[4nda]] - MjNTyrRS (mutant) + nitro-Tyr 
*'''Val-RS'''
**[[4xkz]] - hLysRS C-terminal 
**[[1iyw]] - TtValRS 
**[[1wk9]], [[1wka]] – TtValRS CP1 domain 
**[[1ivs]] – TtValRS + Val-SA + Val-tRNA 
**[[1gax]] - TtValRS + Val-adenylate analog + Val-tRNA 
*Class II aaRS
*'''Ala-RS'''
**[[5t76]], [[4xem]] - hAlaRS catalytic domain 
**[[4xeo]] - hAlaRS catalytic domain (mutant) 
**[[5t5s]], [[5t76]] - hAlaRS residues 757-965 
**[[6nlq]], [[6nly]], [[6now]] - hAlaRS C-terminal 
**[[3g98]] – AaAlaRS residues 758-867 
**[[1riq]] - AaAlaRS catalytic fragment 
**[[2zze]], [[2zzf]], [[1wnu]], [[1wxo]], [[1v4p]], [[1v7o]] – PhAlaRS 
**[[2zvf]] – AfAlaRS C-terminal 
* ''Ala-RS + small substrates or analogs''
**[[5v59]] - hAlaRS + AZ-SA 
**[[3hxu]], [[3hxv]], [[3hxw]] – EcAlaRS catalytic fragment + aa-adenylate 
**[[3hxz]], [[3hy0]], [[3hy1]] - EcAlaRS catalytic fragment (mutant) + aa-adenylate 
**[[3hxx]] - EcAlaRS catalytic fragment + AMPPCP 
**[[3hxy]] - EcAlaRS catalytic fragment + AMPPCP + Ala-AMP + PCP 
**[[3htz]] - AaAlaRS residues 2-454 + Ser 
**[[1yfr]] – AaAlaRS + ATP 
**[[1yfs]] – AaAlaRS + Ala 
**[[1yft]], [[1ygb]] - AaAlaRS catalytic fragment + aa 
**[[2zzg]] - PhAlaRS + Ala-SA 
**[[2ztg]]– AfAlaRS + Ala-SA 
*''Ala-RS + tRNA''
**[[3wqy]], [[3wqz]] – AfAlaRS + Ala-tRNA + Ala-SA 
*'''Asp-RS'''
**[[4j15]], [[4ah6]] - hAspRS 
**[[1eov]] - yAspRS 
**[[3nen]], [[1b8a]] – TkAspRS - ''Thermococcus kodakarensis'' 
**[[3i7f]] – EhAspRS 
**[[1wyd]] – AspRS – ''Sulfolobus tokodaii'' 
**[[1n9w]], [[1l0w]], [[1g51]] – TtAspRS 
**[[1eqr]] – EcAspRS 
**[[5gro]] – HpAspRS N terminal 
**[[4rmf]] – MsAspRS 
**[[6wom]] – ElAspRS 
* ''Asp-RS + small substrates or analogs''
**[[3nel]] – TkAspRS + Asp 
**[[3nem]] - TkAspRS + Asp-adenylate 
**[[5w25]] – MtAspRS + Asp 
**[[4o2d]] – MsAspRS + Asp 
* ''Asp-RS + tRNA''
**[[1asy]], [[1asz]] – yAspRS + Asp-tRNA 
**[[3kfu]], [[1efw]] – TtAspRS + tRNA 
* ''Asp-RS complex''
**[[5y6l]] - hAspRS + MetRS + Glu/ProRS + P18 + P38 
**[[6iy6]] - hAspRS + AIMP2 + Glu/ProRS residues 1-157 
**[[1il2]], [[1c0a]] – EcAspRS + Asp-tRNA + Asp-adenylate 
**[[7ap4]] – TtAspRS + inhibitor 
**[[6hhv]], [[6hhw]] – TtAspRS + Asp-SU 
**[[6hhx]] – TtAspRS + Asp-SC 
**[[6sjc]] – TtAspRS + Asp-SA 
**[[4wj4]] – PaAspRS + Asn-tRNA + Asp 
**[[4wj3]] – PaAspRS + Asn-tRNA + amidotransferase 
*'''Asn-RS'''
**[[5xix]] - hAsnRS 
**[[4zya]] - hAsnRS N terminal 
**[[1x56]] - PhAsnRS 
**[[2kqr]] – BmAsnRS N-terminal – NMR – ''Brugia malayi'' 
**[[6pqh]] – ElAsnRS 
* ''Asn-RS + small substrates or analogs''
**[[2xti]] – BmAsnRS catalytic fragment + Asn-adenine analog 
**[[2xgt]] - BmAsnRS catalytic fragment + Asn-SA 
**[[1x54]] – PhAsnRS + Asn-adenylate 
**[[1x55]] - PhAsnRS + Asn-SA 
**[[11as]] – EcAsnRS + Asn 
**[[12as]] - EcAsnRS + Asn + AMP 
**[[3rl6]] - PaAsnRS + Asn + AMP 
*'''Gly-RS'''
**[[2q5h]] – hGlyRS residues 55-739 
**[[2q5i]], [[4kqe]] - hGlyRS residues 55-739 (mutant) 
**[[2pme]] – hGlyRS 
**[[2pmf]] – hGlyRS (mutant) 
**[[1j5w]] – TmGlyRS chain 
**[[1ati]] – TtGlyRS 
**[[3rf1]] - CjGlyRS a subunit 
* ''Gly-RS + small substrates or analogs''
**[[2zt5]], [[2zxf]] – hGlyRS residues 55-739 + bis-adenosine tetraphosphate 
**[[2zt6]] - hGlyRS residues 55-739 + AMPCPP 
**[[2zt7]] - hGlyRS residues 55-739 + Gly + ATP 
**[[2zt8]] - hGlyRS residues 55-739 + Gly-AMP analog 
**[[1b76]] – TtGlyRS + ATP 
**[[1ggm]] – TtGlyRS + Gly-adenylate 
**[[5f5w]] - AaGlyRS + Gly-adenylate 
**[[3ufg]] - CjGlyRS + ATP 
**[[7eiv]] - EcGlyRS + ANP + Gly 
* ''Gly-RS + tRNA''
**[[5e6m]], [[4qei]], [[4kr2]] - hGlyRS + Gly-tRNA 
**[[4kr3]] - hGlyRS (mutant) + Gly-tRNA 
*'''His-RS'''
**[[4x5o]], [[4g84]], [[4g85]], [[6o76]] - hHisRS 
**[[5w6m]] - hHisRS (mutant) 
**[[1x59]], [[2lw7]] – hHisRS WHEP-TRS domain - NMR 
**[[1htt]] - EcHisRS 
**[[3net]] – HisRS – ''Nostoc'' 
**[[1h4v]] – TtHisRS 
**[[1qe0]] – SaHisRS 
**[[3hri]] – TbHisRS 
**[[1wu7]] – HisRS – ''Thermoplasma acidophilum'' 
* ''His-RS + small substrates or analogs''
**[[4phc]] - hHisRS + His 
**[[3lc0]] – TcHisRS residues 45-478 + His – ''Trypanosoma cruzi'' 
**[[4yp0]], [[4ypf]], [[4yrc]], [[4yrr]], [[4yrs]] - TcHisRS + quinoline derivative 
**[[4yre]], [[4yrj]], [[4yrk]], [[4yrp]] - TcHisRS + phenyl derivative 
**[[4yrg]], [[4yrm]], [[4yrn]], [[4yro]] - TcHisRS + pyridine derivative 
**[[4yrl]] - TcHisRS + aniline derivative 
**[[4yrq]] - TcHisRS + chromenone derivative 
**[[4yrt]] - TcHisRS + naphthalene derivative 
**[[4rdx]] – TtHisRS + tRNA 
**[[1adj]] – TtHisRS + His 
**[[3hrk]] - TbHisRS + His-adenylate 
**[[2el9]] - EcHisRS + His-SA 
**[[1kmm]], [[1ady]] - EcHisRS + His-adenylate 
**[[1kmn]] - EcHisRS + His-ol + ATP 
**[[5e3i]] - AbHisRS + His + ATP 
**[[4e51]] - BtHisRS + His 
*'''Phe-RS'''
**[[3l4g]], [[3cmq]] – hPheRS 
**[[5mgw]], [[5mgh]], [[5mgu]], [[5mgv]] – hPheRS (mutant) 
**[[1pys]] – TtPheRS 
**[[2cxi]] – PhPheRS β chain N-terminal 
**[[3ica]] – PheRS β chain – ''Porphyromonas gingivalis'' 
**[[4p71]] – PaPheRS α+β chain 
**[[3ig2]] – PheRS β chain – ''Bacterioides fragilis'' 
**[[7daw]] – MtPheRS + α+β chains 
**[[6p24]] – EcPheRS + α+β chains 
**[[7n8y]] - SePheRS + chains – ''Salmonella enterica'' 
* ''Phe-RS + small substrates or analogs''
**[[3hfv]] – hPheRS + Tyr 
**[[3teg]] – hPheRS + L-DOPA 
**[[3pco]] – EcPheRS + phenylalanine+ AMP 
**[[6oz5]], [[6p26]] – EcPheRS α+β chains + inhibitor 
**[[3hfz]], [[2amc]] – TtPheRS α+β chains + Tyr 
**[[2akw]], [[1b70]] - TtPheRS α+β chains + Phe 
**[[4tva]] - TtPheRS α+β chains + Phe + puromycin 
**[[3teh]] - TtPheRS α+β chains + L-DOPA 
**[[1jjc]], [[1b7y]] - TtPheRS α+β chains + Phe-adenylate 
**[[2aly]] - TtPheRS α+β chains + Phe-SA 
**[[2rhq]], [[2rhs]] – PheRS α+β+ chains (mutant) + inhibitor – ''Staphylococcus haemolyticus'' 
**[[4p72]], [[4p73]], [[4p74]], [[4p75]] – PaPheRS α+β chains + inhibitor 
**[[7db7]], [[7db8]] – MtPheRS α+β chains + inhibitor 
**[[6p8t]] – AbPheRS α+β chains + inhibitor 
**[[7dpi]] – PfPheRS + α+β chains + inhibitor 
* ''Phe-RS + tRNA''
**[[3tup]] – hPheRS + Phe-tRNA 
**[[1eiy]] - TtPheRS α+β chains + Phe-tRNA 
**[[2iy5]] - TtPheRS α+β chains + Phe-ol + Phe-tRNA 
**[[7k98]], [[7k9m]], [[7ka0]] - MtPheRS + chains + Phe-tRNA + Phe-AMS 
**[[7kab]] - MtPheRS + chains + Phe-tRNA + Phe 
*'''Pro-RS'''
**[[4k86]] – hProRS residues 1000-1512 
**[[1hc7]] – TtProRS 
**[[2i4l]] – RpProRS – ''Rhodopseudomonas palustris'' 
**[[1nj2]] - MtProRS –'' Methanothermobacter thermautotrophicus'' 
**[[1nj8]] – MjProRS 
**[[5xif]], [[6aa0]] – TgProRS residues 334-830 
**[[5ucm]] – PaProRS 
**[[4twa]], [[4ncx]] – PfProRS residues 249-746 
* ''Pro-RS + small substrates or analogs''
**[[3ial]] – GlProRS residues 34-542 + Pro-adenylate 
**[[2i4m]], [[2i4n]] – RpProRS + aa-SA 
**[[2i4o]] – RpProRS + ATP 
**[[2j3l]] – EfProRS + Pro-SA – ''Enterococcus faecalis'' 
**[[1nj1]], [[1nj5]], [[1nj6]] – MtProRS + aa-SA 
**[[1h4t]] - TtProRS + Pro 
**[[5ifu]] – PfProRS residues 249-746 + glyburide 
**[[4wi1]], [[6t7k]], [[7qc1]] – PfProRS residues 249-746 + inhibitor 
*''Pro-RS ternary complex''
**[[4k87]] – hProRS residues 1000-1512 + proline + adenosine 
**[[4k88]] – hProRS residues 1000-1512 + halofunginone 
**[[1h4q]] - TtProRS + Pro-tRNA + Pro-ol 
**[[1h4s]] - TtProRS + Pro-tRNA + Pro-SA 
**[[2j3m]] – EfProRS + Pro-ol + ATP 
**[[5f9z]] – CpProRS residues 186-688 + halofuginone + AMPPNP 
**[[5f9y]] – CpProRS residues 186-688 + proline + AMP 
**[[5xio]] – CpProRS residues 225-719 + halofuginone + ANP 
**[[5znj]] – SaProRS + halofuginone + ANP 
**[[5znk]] – SaProRS + inhibitor + ANP 
**[[6nab]] - NfProRS + Pro + AMP – ''Naegleria fowleri'' 
**[[6uyh]] – NfProRS + halofuginone + ANP 
**[[5xiq]] – TgProRS residues 334-830 + halofuginone + ANP 
**[[7evu]], [[7f9u]], [[7f9v]] – TgProRS residues 215-711 + halofuginone + inhibitor 
**[[7f9r]] – TgProRS residues 215-711 + febrifugine + inhibitor + Pro 
**[[7evv]], [[7fal]] – TgProRS residues 215-711 + inhibitor + Pro 
**[[5xik]], [[6a88]] – TgProRS residues 334-830 + febrifugine derivative + ANP 
**[[5xig]], [[5xih]], [[5xij]] – TgProRS residues 334-830 + inhibitor + ANP 
**[[5xii]] – TgProRS residues 334-830 (mutant) + inhibitor + ANP 
**[[4ydq]], [[4q15]], [[4olf]] – PfProRS residues 254-746 + halofuginone + AMPPNP 
**[[7qb7]], [[7qc2]] – PfProRS residues 249-746 + inhibitor + Pro 
*'''Bifunctional RS''' (bifunctional glutamate/proline tRNA ligase)
**[[4hvc]] – hGlu/ProRS residues 1003-1513 + halofunginone + ATP analog 
**[[5v58]] – hGlu/ProRS residues 1003-1513 + AZ-SA 
**[[5vad]] – hGlu/ProRS residues 1003-1513 + inhibitor 
**[[7osy]] – hGlu/ProRS residues 1003-1513 + Pro 
**[[7bbu]], [[7f98]], [[7f99]], [[7f9a]], [[7f9b]], [[7f9c]], [[7f9d]], [[7osz]], [[7ot0]], [[7ot1]], [[7ot2]], [[7ot3]] – hGlu/ProRS residues 1003-1513 + inhibitor + Pro 
**[[7x09]], [[7x1o]] – hGlu/ProRS residues 1003-1513 + inhibitor + halofuginone 
**[[7y1w]], [[7y28]], [[7y3s]] – hGlu/ProRS residues 1003-1513 + inhibitor + ATP 
**[[5a1n]], [[5a34]], [[5a5h]] – hGlu/ProRS GST-like domain 1-175 + EPRS-AIMP2 
**[[1fyj]] – hGlu/ProRS 677-733 – NMR 
*'''Pyrrolysyl-RS''' see [[Pyrrolysyl-tRNA synthetase]]
*'''Ser-RS'''
**[[3vbb]] - hSerRS 
**[[6gir]] - SerRS – ''Arabidopsis thaliana'' 
**[[3lsq]] – TbSerRS 
**[[1sry]] - TtSerRS 
**[[3lss]] – TbSerRS + ATP 
**[[3err]] – TtSerRS/dynein heavy chain 
**[[2zr3]] – PhSerRS 
**[[2dq3]] – AaSerRS 
**[[2du7]] – MjSerRS 
**[[2odr]] – MemSerRS – ''Methanococcus maripaludis'' 
**[[2cim]] – MbSerRS – ''Methanosarcina barkeri'' 
**[[3qne]], [[3qo5]], [[3qo7]], [[3qo8]] - CaSerRS 
* ''Ser-RS + small substrates or analogs''
**[[4l87]] - hSerRS + Ser-SA 
**[[1wle]] – bSerRS + Ser-adenylate - bovine 
**[[2zr2]] – PhSerRS + ATP 
**[[2dq0]] – PhSerRS + Ser-SA 
**[[2cj9]] – MbSerRS + Ser-SA 
**[[2cjb]] – MbSerRS + Ser 
**[[2cja]] – MbSerRS + ATP 
**[[1ses]], [[1set]] – TtSerRS + Ser-adenylate analog 
**[[6r1m]], [[6r1n]] – SaSerRS + Ser-SA 
**[[6hdz]], [[6he1]], [[6hhy]], [[6hi0]] – PaSerRS + Ser-SU 
**[[6he3]], [[6hhz]] – PaSerRS + Ser-SC 
**[[6r1o]] – EcSerRS + Ser-SA 
**[[6h9x]] – KpSerRS + Ser-SA 
**[[7ap1]] – KpSerRS + inhibitor 
**[[6ote]] – CpSerRS + Ser-SA 
**[[6x94]] – MmSerRS + Ser-SA 
* ''Ser-RS + tRNA''
**[[4rqf]] - hSerRS + SeCys-tRNA 
**[[4rqe]] - hSerRS (mutant) + SeCys-tRNA 
**[[3w3s]] - SerRS (mutant) + SeCys-tRNA + Ser-SA – ''Methanopyrus kandleri'' 
**[[1ser]] – TtSerRS + Ser-tRNA 
*'''PhosphoSer-RS'''
**[[2du4]] - AfPSerRS + Cys-tRNA 
**[[2du3]], [[5x6c]] – AfPSerRS + Cys-tRNA + phosphoserine 
**[[2du5]], [[2du6]] - AfPSerRS (mutant) + Cys-tRNA + phosphoserine 
**[[2odr]] - MemPSerRS 
*'''Thr-RS'''
**[[1wwt]] – hThrRS TGS domain – NMR 
**[[3ugq]], [[3ugt]] - yThrRS 
**[[1y2q]] - PabThrRS editing domain 1-143 
**[[1tje]] - EcThrRS editing domain 1-224 
**[[7l3o]] RBD 330-763 - CpThrRS 
* ''Thr-RS + small substrates or analogs''
**[[4p3n]] - hThrRS editing domain 322-723 + borrelidin 
**[[4hws]] - hThrRS editing domain + inhibitor 
**[[3uh0]] - yThrRS editing domain + Thr-SA 
**[[4eo4]] - yThrRS editing domain + Ser-SA 
**[[3pd2]], [[3pd3]], [[3pd4]], [[3pd5]] – PabThrRS editing domain + aa-aminoadenosine 
**[[2hkz]] – PabThrRS editing domain + Ser 
**[[2hl0]], [[2hl1]] - PabThrRS editing domain + Ser-adenylate 
**[[2hl2]] - PabThrRS editing domain + Ser-SA 
**[[1tke]] - EcThrRS editing domain + Ser 
**[[1tkg]] - EcThrRS editing domain + Ser-SA 
**[[1tky]] - EcThrRS editing domain + Ser-adenylate 
**[[4p3o]], [[4p3p]] - EcThrRS editing domain + borrelidin 
**[[4hwo]], [[4hwp]], [[4hwr]], [[4hws]] - EcThrRS editing domain + inhibitor 
**[[1fyf]], [[1evl]] - EcThrRS catalytic and anticodon-binding domains + aa-SA 
**[[1evk]] - EcThrRS catalytic and anticodon-binding domains + Thr 
**[[1nyq]] – SaThrRS + Thr-SA 
**[[1nyr]] – SaThrRS + ATP 
**[[4s02]], [[4s03]], [[4s0i]], [[4s0j]], [[4s0k]], [[4s0l]] - PabThrRS (mutant) + bi-Phe 
**[[4rrq]] - PabThrRS editing domain + Ser 
**[[4rrr]] - PabThrRS editing domain + Thr 
**[[4rrf]] - MjThrRS editing domain + Ser 
**[[4rrg]] - MjThrRS editing domain + Thr 
**[[6l2q]], [[7cbg]], [[7cbi]], [[7cbh]], [[7wm7]], [[7wmf]], [[7wmi]] - SeThrRS 222-622 + inhibitor 
* ''Thr-RS + tRNA''
**[[4yye]] - yThrRS + Thr-tRNA + Thr-SA 
**[[1qf6]] – EcThrRS + Thr-tRNA
**[[1kog]] – EcThrRS catalytic and anticodon-binding domains + mRNA 

}}
[[Category: Topic Page]]

Pyrrolysyl-tRNA synthetase

2026-08-25T09:51:50Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='Sandbox_166/Scene_2/1' caption='Pyrrolysyl-tRNA synthetase complex with ATP analog and tert-butoxycarbo-lysine (PDB code [[2zin]])'>
__TOC__
== Function ==
[[Pyrrolysyl-tRNA synthetase]] (PyIRS) or '''Pyrrolysyl-tRNA ligase''' is encoded by the gene pyIS and is found to belong as a part of the group of enzymatic proteins whose role involves the cellular process of tRNA aminoacylation required for protein translation.<ref name="trans"> PMID:17267409 </ref> In particular, PyIRS is required for the activation of the amino acid [[Pyrrolysine]] as it associates with a tRNA generating a specific tRNAPyl, which is then further used to transfer the amino acid to a growing polypeptide.<ref name="pept"> PMID:19022179 </ref> The involvement of PyIRS is carried out due to the anticodon CUA on the suppressor tRNAPyl that is complementary to the UAG codon.<ref name="amber"> PMID:1796745 </ref> <ref>PMID:15314242 </ref> The interesting fact is that this is done by the response of the codon UAG (amber codon) on the mRNA that is normally a stop codon in other organisms. Pyrrolysine (Pyl) is the 22nd existing amino acid genetically encoded in nature that was first discovered as a byproduct contained by the active site of monomethylamine methyltransferase, exclusively from Methanosarcina barkeri (M. barkeri) species.<ref name="pept" /> <ref name="barkeri"> PMID:19118381 </ref> Thus, it is utilized by a variety of organisms that metabolize methylamines for acquiring energy such as methanogenic Archaea of the family Methanosarcinace; along with two known bacterium species<ref name="trans" /> <ref name="barkeri" /> Pyrrolysine’s structural makeup consists of 4-methylpyrroline-5-carboxylate in amide linkage with the Nϵ of lysine.<ref name="lysine">PMID:16096277 </ref> This arrangement is comparable to lysine; however, being its derivative it contains an added pyrroline ring that is found to lie situated at the back of the structure.<ref name="lysine" />

In addition, by observing M. barkeri cellular mechanisms containing PyIRS it was detected that it furthermore has the capability to activate an assortment of other imitative of pyrrolysine/lysine; as well as amino acids that are non-canonical.<ref>PMID:17126325 </ref> These amino acids can then be further added to their specialized tRNAPyl; inventing new polypeptides.<ref name="barkeri" /> This procedure is performed by extracting PyIRS, and the amber suppressor tRNAPyl from Methanosarcina. When obtained it must be ensured that the PyIRS-tRNAPyl pair are going to perform their specific roles with the selected amino acids to produce polypeptides containing them.<ref name="amber" /> Thus, their structural components are manipulated and then experimentally designed for the recognition and for the unique aminoacylation intended for it.<ref name="amber" /> Once this has been completed it then is carefully placed into a bacterium species such as Escherichia coli (E. coli).<ref name="amber" /> The reason that this is successful is because once inserted tRNAPyl function as an orthogonal pair with aaRS-tRNA that will not interfere with cellular mechanisms and other components of translation.<ref name="pept" /> <ref name="amber" /> Some of the lysine derivatives such as AcLys, ZLys, BocLys, AlocLys and AzZLys have been experimentally trialed and as a result, have been successfully translated into proteins.<ref name="amber" /> In particular interest, Nϵ-(tert-butyloxycarbonyl –L-lysine (BocLys) is a non-natural amino acid that is a deviation from the structure of lysine which can be intergraded into polypeptides utilizing the amber codon by the process of being esterified to tRNAPyl by PyIRS in E.coli for the incorporation into proteins.<ref name="pept" /> By using this method we can obtain proteins with manipulated structures and functions that can serve useful purposes in studying cellular processes and in altering further mechanisms. See also [[Ligases]].

==Structure==
<scene name='Sandbox_166/2ndstructure/3'>Showing the chains and bound BocLys</scene> ([[2zin]]).
Pyrrolysyl-tRNA synthetase (PyIRS) catalytic complex attached with <scene name='Sandbox_166/2ndstructure/6'>BocLys</scene>, and along with adenosine 5’ (beta, gamma-imido) triphosphate (AMMPPNP) demonstrates the now known structural components and configuration that is needed for the efficient recognition of amino acids and the aminoacylation by PyIRS.<ref name="pept" /> As shown in figure 1, it consists of a multi domain polypeptide made of 1 chain (Chain A) comprising of a total length of 291 residues with 2 catalytic domains; PRK06253 and class_II_aaRS-like_core t.<ref name="pept" /> Furthermore, the structure is observed to consisting of 9 <scene name='Sandbox_166/2ndstructure/1'>α-helices</scene> (95 residues) making 32% of the structure, and the remaining is 12 <scene name='Sandbox_166/2ndstructure/2'>β-strands</scene> (59 residues) consisting of 20% of the other structure. In addition, its structure components require the presence of the 4 ligands; ANP, EDO, LBY, and MG for the protein to correctly perform its biological function.

PyIRS structure is found to enclose a hydrophobic interior where the catalytic activity of recognition and activation of the amino acids is going to take place.<ref name="paper"> PMID:18387634 </ref> This area creates a suitable environment for the binding to occur and for accommodating the residues of pyrrolysine methyl-pyrroline ring inside so it has the capability so further interact with the active-side residues available.<ref name="paper" /> It has been shown, that in order for the amino acid to successfully come in contact proper size of PyIRS must be incorporated at the Nϵ-carbonyl group.<ref name="pept" /> By using the Fo-Fc omit map and with the visible electron density in the active site it was experimentally trialed that the Nϵ-Boc group is situated in the hydrophobic interior in the similar was as the already observed traditional pyrrolysine AMPPNP bound arrangement.<ref name="pept" /> For that reason having the Nϵ-BocLys positioned in this way it has the capability to participate in the hydrogen bonding with Asn346 amide group.<ref name="pept" /> This Asn346 is important when the amino acid is binding because it helps attach its carbonyl side chain; as well as the main-chain α-amino group to ensure the proper recognition it going to take place.<ref name="paper" /> From this Asn346 will also allow the substrate to effectively bind to the side chain amide group by inducible fitting the carbonyl group of the substrate into position.<ref name="pept" /> Next, the Cα-carbonyl groups of BocLys in turn will hydrogen bond Asn346 contrary to the α-amino group which is linked to α-phosphate group of AMPPNP.<ref name="pept" /> Additionally, the BocLys α-carboxyl group is directed to that it is associated outside from the active site allowing for the flexibility due to the ability to rotate around the Cɑ- Cβ bond.<ref name="pept" /> Furthermore, this active site contains an abundant of functional residues such as Lys192, Arg197, Arg217, Lys336, Lys435, Lys438 and Arg439 from the one domain and Arg310, Lys311 and Arg314 from the other, which participate in the effective binding with the tRNA.<ref name="paper" />

==Mechanism==

The proposed mechanism for the insertion of pyrrolysine into polypeptides initially begins with the activation of a special tRNA.<ref name="code"> PMID:12121639 </ref> This is completed by the charging of the 3' CCA end of tRNA as it interacts with lysine via aminoacylation by PyIRS in the presence of the exchange of ATP for AMP and PPi (inorganic pyrophosphate).<ref name="code" /> <ref name="paper" /> When ATP binds to PyIRS it causes a conformational change allowing this to happen.<ref name="paper" /> This will generate lysyl-tRNACUA which is then pre-translationally customized by the influence of the genes PyIB, PyIC and PyID generating Pyl-tRNACUA<ref name="code" /> This specific tRNAPyl is used to transport the amino acid pyrrolysine to the A-site located in the ribosome which is then added to the co-translated polypeptide chain.<ref name="code" /> To ensure the appropriate amino acid find its way to PyIRS, and not to any other class II aaRS present, PyIRS has special identification systems associated with it.<ref name="pept" /> These include special features such as its overall dimension, its structural layout and its binding ability to the hydrophibic active site.<ref name="pept" />

==3D structures of pyrrolysyl-tRNA synthetase==

[[pyrrolysyl-tRNA synthetase 3D structures]]

==Additional Resources==
For Additional information, see: [[Translation]] 

=References=
<references/>
</StructureSection>
[[Category:Topic Page]]

Pyrrolysyl-tRNA synthetase 3D structures

2026-08-25T09:44:00Z

Michal Harel:

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyrrolysyl-tRNA synthetase

**[[6ezd]], [[6jp2]] – CmPTS – ''Candidatus methanomethylophilius'' 
**[[2e3c]], [[8ris]] – MmPTS catalytic domain 185-454 – ''Methanosarcina mazei'' 
**[[2znj]], [[3dsq]] – DhPTS – ''Desulfitobacterium hafniense'' 
**[[7r6o]], [[8ifj]] – PTS – ''Methanogenic archaon<''br />

*Pyrrolysyl-tRNA synthetase binary complex

**[[8c49]] – CmPTS + ANP 
**[[2q7e]], [[3vqw]] – MmPTS catalytic domain + ANP 
**[[4bw9]], [[4cs4]], [[5k1p]], [[5k1x]] – MmPTS catalytic domain (mutant) + ANP 
**[[3vqx]] – MmPTS catalytic domain (mutant) + AMP 
**[[4bwa]] – MmPTS catalytic domain (mutant) + norbornene 
**[[4ch3]], [[4ch4]], [[4ch5]], [[4ch6]] – MmPTS catalytic domain + Lys derivative 
**[[5ud5]] – MmPTS tRNA-binding domain 1-101 + tRNA 
**[[5v6x]] – MmPTS tRNA-binding domain (mutant) + tRNA 
**[[2zni]] – DhPTS + tRNA 

*Pyrrolysyl-tRNA synthetase ternary complex

**[[7u0r]] – CmPTS (mutant) + malonate derivative + ANP 
**[[2zce]], [[2zim]] – MmPTS catalytic domain + pyrrolysine + ANP 
**[[2q7h]] – MmPTS catalytic domain + pyrrolysine + POP 
**[[2q7g]] – MmPTS catalytic domain + pyrrolysine + ATP 
**[[6aaz]], [[6ab8]], [[6abk]], [[6abl]] – MmPTS catalytic domain (mutant) + Lys + ATP 
**[[2zio]], [[3vqv]] – MmPTS catalytic domain + Lys-AMP + PNP 
**[[2zin]], [[3vqy]] – MmPTS catalytic domain + Lys + ANP 
**[[4q6g]] – MmPTS catalytic domain (mutant) + Lys + ADPNP 
**[[6aac]], [[6aad]], [[6aan]], [[6aao]], [[6aaq]], [[6ab0]], [[6ab1]], [[6ab2]], [[6abm]] – MmPTS catalytic domain (mutant) + Lys + ATP 
**[[6aap]] – MmPTS catalytic domain (mutant) + Cys + ATP 
**[[3qtc]] – MmPTS catalytic domain + Tyr + ANP 
**[[7rsm]] – MmPTS catalytic domain + Phe + ANP 
**[[4tqd]] – MmPTS catalytic domain + Phe + ATP 
**[[8ke1]], [[8ke2]], [[8ke3]], [[8ke4]], [[8ke5]], [[8ke6]] – MmPTS catalytic domain (mutant) + Phe + ANP 
**[[6ly7]], [[6lya]] – MmPTS catalytic domain (mutant) + Trp + ANP 
**[[6ly3]], [[6ly6]], [[6lyb]] – MmPTS catalytic domain (mutant) + Ala + ANP 
**[[4cs3]] – MmPTS catalytic domain (mutant) + amino acid + AMP + POP 
**[[4tqf]] – MmPTS catalytic domain + Ala + ATP 
**[[4zib]] – MmPTS catalytic domain (mutant) + Ala + ATP 
**[[8dqg]], [[8dqh]], [[8dqi]] – CmPTS + acridone + ANP 
**[[8dqj]] – CmPTS + acridone + ATP 
}}
[[Category:Topic Page]]

Pyrrolysyl-tRNA synthetase 3D structures

2026-08-25T09:42:17Z

Michal Harel: Created page with "Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} {{#tree:id=OrganizedByTopic|openlevels=0| *Pyrrolysyl-tRNA synthetase **6ezd, 6jp2 – CmPTS – ''Candidatus methanomethylophilius'' **2e3c, 8ris – MmPTS catalytic domain 185-454 – ''Methanosarcina mazei'' **2znj, 3dsq – DhPTS – Desulfitobacterium hafniense **7r6o, 8ifj – PTS – Methanogenic archaon Pyrrolysyl-tRNA synthetas..."

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyrrolysyl-tRNA synthetase

**[[6ezd]], [[6jp2]] – CmPTS – ''Candidatus methanomethylophilius'' 
**[[2e3c]], [[8ris]] – MmPTS catalytic domain 185-454 – ''Methanosarcina mazei'' 

**[[2znj]], [[3dsq]] – DhPTS – Desulfitobacterium hafniense 
**[[7r6o]], [[8ifj]] – PTS – Methanogenic archaon 

Pyrrolysyl-tRNA synthetase binary complex

**[[8c49]] – CmPTS + ANP 
**[[2q7e]], [[3vqw]] – MmPTS catalytic domain + ANP 
**[[4bw9]], [[4cs4]], [[5k1p]], [[5k1x]] – MmPTS catalytic domain (mutant) + ANP 
**[[3vqx]] – MmPTS catalytic domain (mutant) + AMP 
**[[4bwa]] – MmPTS catalytic domain (mutant) + norbornene 
**[[4ch3]], [[4ch4]], [[4ch5]], [[4ch6]] – MmPTS catalytic domain + Lys derivative 
**[[5ud5]] – MmPTS tRNA-binding domain 1-101 + tRNA 
**[[5v6x]] – MmPTS tRNA-binding domain (mutant) + tRNA 
**[[2zni]] – DhPTS + tRNA 

Pyrrolysyl-tRNA synthetase ternary complex

**[[7u0r]] – CmPTS (mutant) + malonate derivative + ANP 
**[[2zce]], [[2zim]] – MmPTS catalytic domain + pyrrolysine + ANP 
**[[2q7h]] – MmPTS catalytic domain + pyrrolysine + POP 
**[[2q7g]] – MmPTS catalytic domain + pyrrolysine + ATP 
**[[6aaz]], [[6ab8]], [[6abk]], [[6abl]] – MmPTS catalytic domain (mutant) + Lys + ATP 
**[[2zio]], [[3vqv]] – MmPTS catalytic domain + Lys-AMP + PNP 
**[[2zin]], [[3vqy]] – MmPTS catalytic domain + Lys + ANP 
**[[4q6g]] – MmPTS catalytic domain (mutant) + Lys + ADPNP 
**[[6aac]], [[6aad]], [[6aan]], [[6aao]], [[6aaq]], [[6ab0]], [[6ab1]], [[6ab2]], [[6abm]] – MmPTS catalytic domain (mutant) + Lys + ATP 
**[[6aap]] – MmPTS catalytic domain (mutant) + Cys + ATP 
**[[3qtc]] – MmPTS catalytic domain + Tyr + ANP 
**[[7rsm]] – MmPTS catalytic domain + Phe + ANP 
**[[4tqd]] – MmPTS catalytic domain + Phe + ATP 
**[[8ke1]], [[8ke2]], [[8ke3]], [[8ke4]], [[8ke5]], [[8ke6]] – MmPTS catalytic domain (mutant) + Phe + ANP 
**[[6ly7]], [[6lya]] – MmPTS catalytic domain (mutant) + Trp + ANP 
**[[6ly3]], [[6ly6]], [[6lyb]] – MmPTS catalytic domain (mutant) + Ala + ANP 
**[[4cs3]] – MmPTS catalytic domain (mutant) + amino acid + AMP + POP 
**[[4tqf]] – MmPTS catalytic domain + Ala + ATP 
**[[4zib]] – MmPTS catalytic domain (mutant) + Ala + ATP 
**[[8dqg]], [[8dqh]], [[8dqi]] – CmPTS + acridone + ANP 
**[[8dqj]] – CmPTS + acridone + ATP 
}}
[[Category:Topic Page]]

Pyrrolysyl-tRNA synthetase

2026-08-25T09:41:12Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='Sandbox_166/Scene_2/1' caption='Pyrrolysyl-tRNA synthetase complex with ATP analog and tert-butoxycarbo-lysine (PDB code [[2zin]])'>
__TOC__
== Function ==
[[Pyrrolysyl-tRNA synthetase]] (PyIRS) or '''Pyrrolysyl-tRNA ligase''' is encoded by the gene pyIS and is found to belong as a part of the group of enzymatic proteins whose role involves the cellular process of tRNA aminoacylation required for protein translation.<ref name="trans"> PMID:17267409 </ref> In particular, PyIRS is required for the activation of the amino acid [[Pyrrolysine]] as it associates with a tRNA generating a specific tRNAPyl, which is then further used to transfer the amino acid to a growing polypeptide.<ref name="pept"> PMID:19022179 </ref> The involvement of PyIRS is carried out due to the anticodon CUA on the suppressor tRNAPyl that is complementary to the UAG codon.<ref name="amber"> PMID:1796745 </ref> <ref>PMID:15314242 </ref> The interesting fact is that this is done by the response of the codon UAG (amber codon) on the mRNA that is normally a stop codon in other organisms. Pyrrolysine (Pyl) is the 22nd existing amino acid genetically encoded in nature that was first discovered as a byproduct contained by the active site of monomethylamine methyltransferase, exclusively from Methanosarcina barkeri (M. barkeri) species.<ref name="pept" /> <ref name="barkeri"> PMID:19118381 </ref> Thus, it is utilized by a variety of organisms that metabolize methylamines for acquiring energy such as methanogenic Archaea of the family Methanosarcinace; along with two known bacterium species<ref name="trans" /> <ref name="barkeri" /> Pyrrolysine’s structural makeup consists of 4-methylpyrroline-5-carboxylate in amide linkage with the Nϵ of lysine.<ref name="lysine">PMID:16096277 </ref> This arrangement is comparable to lysine; however, being its derivative it contains an added pyrroline ring that is found to lie situated at the back of the structure.<ref name="lysine" />

In addition, by observing M. barkeri cellular mechanisms containing PyIRS it was detected that it furthermore has the capability to activate an assortment of other imitative of pyrrolysine/lysine; as well as amino acids that are non-canonical.<ref>PMID:17126325 </ref> These amino acids can then be further added to their specialized tRNAPyl; inventing new polypeptides.<ref name="barkeri" /> This procedure is performed by extracting PyIRS, and the amber suppressor tRNAPyl from Methanosarcina. When obtained it must be ensured that the PyIRS-tRNAPyl pair are going to perform their specific roles with the selected amino acids to produce polypeptides containing them.<ref name="amber" /> Thus, their structural components are manipulated and then experimentally designed for the recognition and for the unique aminoacylation intended for it.<ref name="amber" /> Once this has been completed it then is carefully placed into a bacterium species such as Escherichia coli (E. coli).<ref name="amber" /> The reason that this is successful is because once inserted tRNAPyl function as an orthogonal pair with aaRS-tRNA that will not interfere with cellular mechanisms and other components of translation.<ref name="pept" /> <ref name="amber" /> Some of the lysine derivatives such as AcLys, ZLys, BocLys, AlocLys and AzZLys have been experimentally trialed and as a result, have been successfully translated into proteins.<ref name="amber" /> In particular interest, Nϵ-(tert-butyloxycarbonyl –L-lysine (BocLys) is a non-natural amino acid that is a deviation from the structure of lysine which can be intergraded into polypeptides utilizing the amber codon by the process of being esterified to tRNAPyl by PyIRS in E.coli for the incorporation into proteins.<ref name="pept" /> By using this method we can obtain proteins with manipulated structures and functions that can serve useful purposes in studying cellular processes and in altering further mechanisms. See also [[Ligases]].

==Structure==
<scene name='Sandbox_166/2ndstructure/3'>Showing the chains and bound BocLys</scene> ([[2zin]]).
Pyrrolysyl-tRNA synthetase (PyIRS) catalytic complex attached with <scene name='Sandbox_166/2ndstructure/6'>BocLys</scene>, and along with adenosine 5’ (beta, gamma-imido) triphosphate (AMMPPNP) demonstrates the now known structural components and configuration that is needed for the efficient recognition of amino acids and the aminoacylation by PyIRS.<ref name="pept" /> As shown in figure 1, it consists of a multi domain polypeptide made of 1 chain (Chain A) comprising of a total length of 291 residues with 2 catalytic domains; PRK06253 and class_II_aaRS-like_core t.<ref name="pept" /> Furthermore, the structure is observed to consisting of 9 <scene name='Sandbox_166/2ndstructure/1'>α-helices</scene> (95 residues) making 32% of the structure, and the remaining is 12 <scene name='Sandbox_166/2ndstructure/2'>β-strands</scene> (59 residues) consisting of 20% of the other structure. In addition, its structure components require the presence of the 4 ligands; ANP, EDO, LBY, and MG for the protein to correctly perform its biological function.

PyIRS structure is found to enclose a hydrophobic interior where the catalytic activity of recognition and activation of the amino acids is going to take place.<ref name="paper"> PMID:18387634 </ref> This area creates a suitable environment for the binding to occur and for accommodating the residues of pyrrolysine methyl-pyrroline ring inside so it has the capability so further interact with the active-side residues available.<ref name="paper" /> It has been shown, that in order for the amino acid to successfully come in contact proper size of PyIRS must be incorporated at the Nϵ-carbonyl group.<ref name="pept" /> By using the Fo-Fc omit map and with the visible electron density in the active site it was experimentally trialed that the Nϵ-Boc group is situated in the hydrophobic interior in the similar was as the already observed traditional pyrrolysine AMPPNP bound arrangement.<ref name="pept" /> For that reason having the Nϵ-BocLys positioned in this way it has the capability to participate in the hydrogen bonding with Asn346 amide group.<ref name="pept" /> This Asn346 is important when the amino acid is binding because it helps attach its carbonyl side chain; as well as the main-chain α-amino group to ensure the proper recognition it going to take place.<ref name="paper" /> From this Asn346 will also allow the substrate to effectively bind to the side chain amide group by inducible fitting the carbonyl group of the substrate into position.<ref name="pept" /> Next, the Cα-carbonyl groups of BocLys in turn will hydrogen bond Asn346 contrary to the α-amino group which is linked to α-phosphate group of AMPPNP.<ref name="pept" /> Additionally, the BocLys α-carboxyl group is directed to that it is associated outside from the active site allowing for the flexibility due to the ability to rotate around the Cɑ- Cβ bond.<ref name="pept" /> Furthermore, this active site contains an abundant of functional residues such as Lys192, Arg197, Arg217, Lys336, Lys435, Lys438 and Arg439 from the one domain and Arg310, Lys311 and Arg314 from the other, which participate in the effective binding with the tRNA.<ref name="paper" />

==Mechanism==

The proposed mechanism for the insertion of pyrrolysine into polypeptides initially begins with the activation of a special tRNA.<ref name="code"> PMID:12121639 </ref> This is completed by the charging of the 3' CCA end of tRNA as it interacts with lysine via aminoacylation by PyIRS in the presence of the exchange of ATP for AMP and PPi (inorganic pyrophosphate).<ref name="code" /> <ref name="paper" /> When ATP binds to PyIRS it causes a conformational change allowing this to happen.<ref name="paper" /> This will generate lysyl-tRNACUA which is then pre-translationally customized by the influence of the genes PyIB, PyIC and PyID generating Pyl-tRNACUA<ref name="code" /> This specific tRNAPyl is used to transport the amino acid pyrrolysine to the A-site located in the ribosome which is then added to the co-translated polypeptide chain.<ref name="code" /> To ensure the appropriate amino acid find its way to PyIRS, and not to any other class II aaRS present, PyIRS has special identification systems associated with it.<ref name="pept" /> These include special features such as its overall dimension, its structural layout and its binding ability to the hydrophibic active site.<ref name="pept" />

==3D structures of pyrrolysyl-tRNA synthetase==

[[pyrrolysyl-tRNA synthetase 3D structures]]

See [[Aminoacyl tRNA Synthetase]]

==Additional Resources==
For Additional information, see: [[Translation]] 

=References=
<references/>
</StructureSection>
[[Category:Topic Page]]

Pyrrolysyl-tRNA synthetase

2026-08-25T09:40:14Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='Sandbox_166/Scene_2/1' caption='Pyrrolysyl-tRNA synthetase complex with ATP analog and tert-butoxycarbo-lysine (PDB code [[2zin]])'>
__TOC__
== Function ==
[[Pyrrolysyl-tRNA synthetase]] (PyIRS) or '''Pyrrolysyl-tRNA ligase''' is encoded by the gene pyIS and is found to belong as a part of the group of enzymatic proteins whose role involves the cellular process of tRNA aminoacylation required for protein translation.<ref name="trans"> PMID:17267409 </ref> In particular, PyIRS is required for the activation of the amino acid [[Pyrrolysine]] as it associates with a tRNA generating a specific tRNAPyl, which is then further used to transfer the amino acid to a growing polypeptide.<ref name="pept"> PMID:19022179 </ref> The involvement of PyIRS is carried out due to the anticodon CUA on the suppressor tRNAPyl that is complementary to the UAG codon.<ref name="amber"> PMID:1796745 </ref> <ref>PMID:15314242 </ref> The interesting fact is that this is done by the response of the codon UAG (amber codon) on the mRNA that is normally a stop codon in other organisms. Pyrrolysine (Pyl) is the 22nd existing amino acid genetically encoded in nature that was first discovered as a byproduct contained by the active site of monomethylamine methyltransferase, exclusively from Methanosarcina barkeri (M. barkeri) species.<ref name="pept" /> <ref name="barkeri"> PMID:19118381 </ref> Thus, it is utilized by a variety of organisms that metabolize methylamines for acquiring energy such as methanogenic Archaea of the family Methanosarcinace; along with two known bacterium species<ref name="trans" /> <ref name="barkeri" /> Pyrrolysine’s structural makeup consists of 4-methylpyrroline-5-carboxylate in amide linkage with the Nϵ of lysine.<ref name="lysine">PMID:16096277 </ref> This arrangement is comparable to lysine; however, being its derivative it contains an added pyrroline ring that is found to lie situated at the back of the structure.<ref name="lysine" />

In addition, by observing M. barkeri cellular mechanisms containing PyIRS it was detected that it furthermore has the capability to activate an assortment of other imitative of pyrrolysine/lysine; as well as amino acids that are non-canonical.<ref>PMID:17126325 </ref> These amino acids can then be further added to their specialized tRNAPyl; inventing new polypeptides.<ref name="barkeri" /> This procedure is performed by extracting PyIRS, and the amber suppressor tRNAPyl from Methanosarcina. When obtained it must be ensured that the PyIRS-tRNAPyl pair are going to perform their specific roles with the selected amino acids to produce polypeptides containing them.<ref name="amber" /> Thus, their structural components are manipulated and then experimentally designed for the recognition and for the unique aminoacylation intended for it.<ref name="amber" /> Once this has been completed it then is carefully placed into a bacterium species such as Escherichia coli (E. coli).<ref name="amber" /> The reason that this is successful is because once inserted tRNAPyl function as an orthogonal pair with aaRS-tRNA that will not interfere with cellular mechanisms and other components of translation.<ref name="pept" /> <ref name="amber" /> Some of the lysine derivatives such as AcLys, ZLys, BocLys, AlocLys and AzZLys have been experimentally trialed and as a result, have been successfully translated into proteins.<ref name="amber" /> In particular interest, Nϵ-(tert-butyloxycarbonyl –L-lysine (BocLys) is a non-natural amino acid that is a deviation from the structure of lysine which can be intergraded into polypeptides utilizing the amber codon by the process of being esterified to tRNAPyl by PyIRS in E.coli for the incorporation into proteins.<ref name="pept" /> By using this method we can obtain proteins with manipulated structures and functions that can serve useful purposes in studying cellular processes and in altering further mechanisms. See also [[Ligases]].

==Structure==
<scene name='Sandbox_166/2ndstructure/3'>Showing the chains and bound BocLys</scene> ([[2zin]]).
Pyrrolysyl-tRNA synthetase (PyIRS) catalytic complex attached with <scene name='Sandbox_166/2ndstructure/6'>BocLys</scene>, and along with adenosine 5’ (beta, gamma-imido) triphosphate (AMMPPNP) demonstrates the now known structural components and configuration that is needed for the efficient recognition of amino acids and the aminoacylation by PyIRS.<ref name="pept" /> As shown in figure 1, it consists of a multi domain polypeptide made of 1 chain (Chain A) comprising of a total length of 291 residues with 2 catalytic domains; PRK06253 and class_II_aaRS-like_core t.<ref name="pept" /> Furthermore, the structure is observed to consisting of 9 <scene name='Sandbox_166/2ndstructure/1'>α-helices</scene> (95 residues) making 32% of the structure, and the remaining is 12 <scene name='Sandbox_166/2ndstructure/2'>β-strands</scene> (59 residues) consisting of 20% of the other structure. In addition, its structure components require the presence of the 4 ligands; ANP, EDO, LBY, and MG for the protein to correctly perform its biological function.

PyIRS structure is found to enclose a hydrophobic interior where the catalytic activity of recognition and activation of the amino acids is going to take place.<ref name="paper"> PMID:18387634 </ref> This area creates a suitable environment for the binding to occur and for accommodating the residues of pyrrolysine methyl-pyrroline ring inside so it has the capability so further interact with the active-side residues available.<ref name="paper" /> It has been shown, that in order for the amino acid to successfully come in contact proper size of PyIRS must be incorporated at the Nϵ-carbonyl group.<ref name="pept" /> By using the Fo-Fc omit map and with the visible electron density in the active site it was experimentally trialed that the Nϵ-Boc group is situated in the hydrophobic interior in the similar was as the already observed traditional pyrrolysine AMPPNP bound arrangement.<ref name="pept" /> For that reason having the Nϵ-BocLys positioned in this way it has the capability to participate in the hydrogen bonding with Asn346 amide group.<ref name="pept" /> This Asn346 is important when the amino acid is binding because it helps attach its carbonyl side chain; as well as the main-chain α-amino group to ensure the proper recognition it going to take place.<ref name="paper" /> From this Asn346 will also allow the substrate to effectively bind to the side chain amide group by inducible fitting the carbonyl group of the substrate into position.<ref name="pept" /> Next, the Cα-carbonyl groups of BocLys in turn will hydrogen bond Asn346 contrary to the α-amino group which is linked to α-phosphate group of AMPPNP.<ref name="pept" /> Additionally, the BocLys α-carboxyl group is directed to that it is associated outside from the active site allowing for the flexibility due to the ability to rotate around the Cɑ- Cβ bond.<ref name="pept" /> Furthermore, this active site contains an abundant of functional residues such as Lys192, Arg197, Arg217, Lys336, Lys435, Lys438 and Arg439 from the one domain and Arg310, Lys311 and Arg314 from the other, which participate in the effective binding with the tRNA.<ref name="paper" />

==Mechanism==

The proposed mechanism for the insertion of pyrrolysine into polypeptides initially begins with the activation of a special tRNA.<ref name="code"> PMID:12121639 </ref> This is completed by the charging of the 3' CCA end of tRNA as it interacts with lysine via aminoacylation by PyIRS in the presence of the exchange of ATP for AMP and PPi (inorganic pyrophosphate).<ref name="code" /> <ref name="paper" /> When ATP binds to PyIRS it causes a conformational change allowing this to happen.<ref name="paper" /> This will generate lysyl-tRNACUA which is then pre-translationally customized by the influence of the genes PyIB, PyIC and PyID generating Pyl-tRNACUA<ref name="code" /> This specific tRNAPyl is used to transport the amino acid pyrrolysine to the A-site located in the ribosome which is then added to the co-translated polypeptide chain.<ref name="code" /> To ensure the appropriate amino acid find its way to PyIRS, and not to any other class II aaRS present, PyIRS has special identification systems associated with it.<ref name="pept" /> These include special features such as its overall dimension, its structural layout and its binding ability to the hydrophibic active site.<ref name="pept" />
</StructureSection>

==3D structures of pyrrolysyl-tRNA synthetase==

[[pyrrolysyl-tRNA synthetase 3D structures]]

See [[Aminoacyl tRNA Synthetase]]

==Additional Resources==
For Additional information, see: [[Translation]] 

=References=
<references/>
</StructureSection>
[[Category:Topic Page]]

Pyrrolysyl-tRNA synthetase

2026-08-25T09:39:05Z

Michal Harel: /* 3D structures of pyrrolysyl-tRNA synthetase */

<StructureSection load='' size='350' side='right' scene='Sandbox_166/Scene_2/1' caption='Pyrrolysyl-tRNA synthetase complex with ATP analog and tert-butoxycarbo-lysine (PDB code [[2zin]])'>
__TOC__
== Function ==
[[Pyrrolysyl-tRNA synthetase]] (PyIRS) or '''Pyrrolysyl-tRNA ligase''' is encoded by the gene pyIS and is found to belong as a part of the group of enzymatic proteins whose role involves the cellular process of tRNA aminoacylation required for protein translation.<ref name="trans"> PMID:17267409 </ref> In particular, PyIRS is required for the activation of the amino acid [[Pyrrolysine]] as it associates with a tRNA generating a specific tRNAPyl, which is then further used to transfer the amino acid to a growing polypeptide.<ref name="pept"> PMID:19022179 </ref> The involvement of PyIRS is carried out due to the anticodon CUA on the suppressor tRNAPyl that is complementary to the UAG codon.<ref name="amber"> PMID:1796745 </ref> <ref>PMID:15314242 </ref> The interesting fact is that this is done by the response of the codon UAG (amber codon) on the mRNA that is normally a stop codon in other organisms. Pyrrolysine (Pyl) is the 22nd existing amino acid genetically encoded in nature that was first discovered as a byproduct contained by the active site of monomethylamine methyltransferase, exclusively from Methanosarcina barkeri (M. barkeri) species.<ref name="pept" /> <ref name="barkeri"> PMID:19118381 </ref> Thus, it is utilized by a variety of organisms that metabolize methylamines for acquiring energy such as methanogenic Archaea of the family Methanosarcinace; along with two known bacterium species<ref name="trans" /> <ref name="barkeri" /> Pyrrolysine’s structural makeup consists of 4-methylpyrroline-5-carboxylate in amide linkage with the Nϵ of lysine.<ref name="lysine">PMID:16096277 </ref> This arrangement is comparable to lysine; however, being its derivative it contains an added pyrroline ring that is found to lie situated at the back of the structure.<ref name="lysine" />

In addition, by observing M. barkeri cellular mechanisms containing PyIRS it was detected that it furthermore has the capability to activate an assortment of other imitative of pyrrolysine/lysine; as well as amino acids that are non-canonical.<ref>PMID:17126325 </ref> These amino acids can then be further added to their specialized tRNAPyl; inventing new polypeptides.<ref name="barkeri" /> This procedure is performed by extracting PyIRS, and the amber suppressor tRNAPyl from Methanosarcina. When obtained it must be ensured that the PyIRS-tRNAPyl pair are going to perform their specific roles with the selected amino acids to produce polypeptides containing them.<ref name="amber" /> Thus, their structural components are manipulated and then experimentally designed for the recognition and for the unique aminoacylation intended for it.<ref name="amber" /> Once this has been completed it then is carefully placed into a bacterium species such as Escherichia coli (E. coli).<ref name="amber" /> The reason that this is successful is because once inserted tRNAPyl function as an orthogonal pair with aaRS-tRNA that will not interfere with cellular mechanisms and other components of translation.<ref name="pept" /> <ref name="amber" /> Some of the lysine derivatives such as AcLys, ZLys, BocLys, AlocLys and AzZLys have been experimentally trialed and as a result, have been successfully translated into proteins.<ref name="amber" /> In particular interest, Nϵ-(tert-butyloxycarbonyl –L-lysine (BocLys) is a non-natural amino acid that is a deviation from the structure of lysine which can be intergraded into polypeptides utilizing the amber codon by the process of being esterified to tRNAPyl by PyIRS in E.coli for the incorporation into proteins.<ref name="pept" /> By using this method we can obtain proteins with manipulated structures and functions that can serve useful purposes in studying cellular processes and in altering further mechanisms. See also [[Ligases]].

==Structure==
<scene name='Sandbox_166/2ndstructure/3'>Showing the chains and bound BocLys</scene> ([[2zin]]).
Pyrrolysyl-tRNA synthetase (PyIRS) catalytic complex attached with <scene name='Sandbox_166/2ndstructure/6'>BocLys</scene>, and along with adenosine 5’ (beta, gamma-imido) triphosphate (AMMPPNP) demonstrates the now known structural components and configuration that is needed for the efficient recognition of amino acids and the aminoacylation by PyIRS.<ref name="pept" /> As shown in figure 1, it consists of a multi domain polypeptide made of 1 chain (Chain A) comprising of a total length of 291 residues with 2 catalytic domains; PRK06253 and class_II_aaRS-like_core t.<ref name="pept" /> Furthermore, the structure is observed to consisting of 9 <scene name='Sandbox_166/2ndstructure/1'>α-helices</scene> (95 residues) making 32% of the structure, and the remaining is 12 <scene name='Sandbox_166/2ndstructure/2'>β-strands</scene> (59 residues) consisting of 20% of the other structure. In addition, its structure components require the presence of the 4 ligands; ANP, EDO, LBY, and MG for the protein to correctly perform its biological function.

PyIRS structure is found to enclose a hydrophobic interior where the catalytic activity of recognition and activation of the amino acids is going to take place.<ref name="paper"> PMID:18387634 </ref> This area creates a suitable environment for the binding to occur and for accommodating the residues of pyrrolysine methyl-pyrroline ring inside so it has the capability so further interact with the active-side residues available.<ref name="paper" /> It has been shown, that in order for the amino acid to successfully come in contact proper size of PyIRS must be incorporated at the Nϵ-carbonyl group.<ref name="pept" /> By using the Fo-Fc omit map and with the visible electron density in the active site it was experimentally trialed that the Nϵ-Boc group is situated in the hydrophobic interior in the similar was as the already observed traditional pyrrolysine AMPPNP bound arrangement.<ref name="pept" /> For that reason having the Nϵ-BocLys positioned in this way it has the capability to participate in the hydrogen bonding with Asn346 amide group.<ref name="pept" /> This Asn346 is important when the amino acid is binding because it helps attach its carbonyl side chain; as well as the main-chain α-amino group to ensure the proper recognition it going to take place.<ref name="paper" /> From this Asn346 will also allow the substrate to effectively bind to the side chain amide group by inducible fitting the carbonyl group of the substrate into position.<ref name="pept" /> Next, the Cα-carbonyl groups of BocLys in turn will hydrogen bond Asn346 contrary to the α-amino group which is linked to α-phosphate group of AMPPNP.<ref name="pept" /> Additionally, the BocLys α-carboxyl group is directed to that it is associated outside from the active site allowing for the flexibility due to the ability to rotate around the Cɑ- Cβ bond.<ref name="pept" /> Furthermore, this active site contains an abundant of functional residues such as Lys192, Arg197, Arg217, Lys336, Lys435, Lys438 and Arg439 from the one domain and Arg310, Lys311 and Arg314 from the other, which participate in the effective binding with the tRNA.<ref name="paper" />

==Mechanism==

The proposed mechanism for the insertion of pyrrolysine into polypeptides initially begins with the activation of a special tRNA.<ref name="code"> PMID:12121639 </ref> This is completed by the charging of the 3' CCA end of tRNA as it interacts with lysine via aminoacylation by PyIRS in the presence of the exchange of ATP for AMP and PPi (inorganic pyrophosphate).<ref name="code" /> <ref name="paper" /> When ATP binds to PyIRS it causes a conformational change allowing this to happen.<ref name="paper" /> This will generate lysyl-tRNACUA which is then pre-translationally customized by the influence of the genes PyIB, PyIC and PyID generating Pyl-tRNACUA<ref name="code" /> This specific tRNAPyl is used to transport the amino acid pyrrolysine to the A-site located in the ribosome which is then added to the co-translated polypeptide chain.<ref name="code" /> To ensure the appropriate amino acid find its way to PyIRS, and not to any other class II aaRS present, PyIRS has special identification systems associated with it.<ref name="pept" /> These include special features such as its overall dimension, its structural layout and its binding ability to the hydrophibic active site.<ref name="pept" />
</StructureSection>

==3D structures of pyrrolysyl-tRNA synthetase==

[[pyrrolysyl-tRNA synthetase 3D structures]]

See [[Aminoacyl tRNA Synthetase]]

==Additional Resources==
For Additional information, see: [[Translation]] 

=References=
<references/>

[[Category:Topic Page]]

Pyrrolysyl-tRNA synthetase

2026-08-25T09:37:57Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='Sandbox_166/Scene_2/1' caption='Pyrrolysyl-tRNA synthetase complex with ATP analog and tert-butoxycarbo-lysine (PDB code [[2zin]])'>
__TOC__
== Function ==
[[Pyrrolysyl-tRNA synthetase]] (PyIRS) or '''Pyrrolysyl-tRNA ligase''' is encoded by the gene pyIS and is found to belong as a part of the group of enzymatic proteins whose role involves the cellular process of tRNA aminoacylation required for protein translation.<ref name="trans"> PMID:17267409 </ref> In particular, PyIRS is required for the activation of the amino acid [[Pyrrolysine]] as it associates with a tRNA generating a specific tRNAPyl, which is then further used to transfer the amino acid to a growing polypeptide.<ref name="pept"> PMID:19022179 </ref> The involvement of PyIRS is carried out due to the anticodon CUA on the suppressor tRNAPyl that is complementary to the UAG codon.<ref name="amber"> PMID:1796745 </ref> <ref>PMID:15314242 </ref> The interesting fact is that this is done by the response of the codon UAG (amber codon) on the mRNA that is normally a stop codon in other organisms. Pyrrolysine (Pyl) is the 22nd existing amino acid genetically encoded in nature that was first discovered as a byproduct contained by the active site of monomethylamine methyltransferase, exclusively from Methanosarcina barkeri (M. barkeri) species.<ref name="pept" /> <ref name="barkeri"> PMID:19118381 </ref> Thus, it is utilized by a variety of organisms that metabolize methylamines for acquiring energy such as methanogenic Archaea of the family Methanosarcinace; along with two known bacterium species<ref name="trans" /> <ref name="barkeri" /> Pyrrolysine’s structural makeup consists of 4-methylpyrroline-5-carboxylate in amide linkage with the Nϵ of lysine.<ref name="lysine">PMID:16096277 </ref> This arrangement is comparable to lysine; however, being its derivative it contains an added pyrroline ring that is found to lie situated at the back of the structure.<ref name="lysine" />

In addition, by observing M. barkeri cellular mechanisms containing PyIRS it was detected that it furthermore has the capability to activate an assortment of other imitative of pyrrolysine/lysine; as well as amino acids that are non-canonical.<ref>PMID:17126325 </ref> These amino acids can then be further added to their specialized tRNAPyl; inventing new polypeptides.<ref name="barkeri" /> This procedure is performed by extracting PyIRS, and the amber suppressor tRNAPyl from Methanosarcina. When obtained it must be ensured that the PyIRS-tRNAPyl pair are going to perform their specific roles with the selected amino acids to produce polypeptides containing them.<ref name="amber" /> Thus, their structural components are manipulated and then experimentally designed for the recognition and for the unique aminoacylation intended for it.<ref name="amber" /> Once this has been completed it then is carefully placed into a bacterium species such as Escherichia coli (E. coli).<ref name="amber" /> The reason that this is successful is because once inserted tRNAPyl function as an orthogonal pair with aaRS-tRNA that will not interfere with cellular mechanisms and other components of translation.<ref name="pept" /> <ref name="amber" /> Some of the lysine derivatives such as AcLys, ZLys, BocLys, AlocLys and AzZLys have been experimentally trialed and as a result, have been successfully translated into proteins.<ref name="amber" /> In particular interest, Nϵ-(tert-butyloxycarbonyl –L-lysine (BocLys) is a non-natural amino acid that is a deviation from the structure of lysine which can be intergraded into polypeptides utilizing the amber codon by the process of being esterified to tRNAPyl by PyIRS in E.coli for the incorporation into proteins.<ref name="pept" /> By using this method we can obtain proteins with manipulated structures and functions that can serve useful purposes in studying cellular processes and in altering further mechanisms. See also [[Ligases]].

==Structure==
<scene name='Sandbox_166/2ndstructure/3'>Showing the chains and bound BocLys</scene> ([[2zin]]).
Pyrrolysyl-tRNA synthetase (PyIRS) catalytic complex attached with <scene name='Sandbox_166/2ndstructure/6'>BocLys</scene>, and along with adenosine 5’ (beta, gamma-imido) triphosphate (AMMPPNP) demonstrates the now known structural components and configuration that is needed for the efficient recognition of amino acids and the aminoacylation by PyIRS.<ref name="pept" /> As shown in figure 1, it consists of a multi domain polypeptide made of 1 chain (Chain A) comprising of a total length of 291 residues with 2 catalytic domains; PRK06253 and class_II_aaRS-like_core t.<ref name="pept" /> Furthermore, the structure is observed to consisting of 9 <scene name='Sandbox_166/2ndstructure/1'>α-helices</scene> (95 residues) making 32% of the structure, and the remaining is 12 <scene name='Sandbox_166/2ndstructure/2'>β-strands</scene> (59 residues) consisting of 20% of the other structure. In addition, its structure components require the presence of the 4 ligands; ANP, EDO, LBY, and MG for the protein to correctly perform its biological function.

PyIRS structure is found to enclose a hydrophobic interior where the catalytic activity of recognition and activation of the amino acids is going to take place.<ref name="paper"> PMID:18387634 </ref> This area creates a suitable environment for the binding to occur and for accommodating the residues of pyrrolysine methyl-pyrroline ring inside so it has the capability so further interact with the active-side residues available.<ref name="paper" /> It has been shown, that in order for the amino acid to successfully come in contact proper size of PyIRS must be incorporated at the Nϵ-carbonyl group.<ref name="pept" /> By using the Fo-Fc omit map and with the visible electron density in the active site it was experimentally trialed that the Nϵ-Boc group is situated in the hydrophobic interior in the similar was as the already observed traditional pyrrolysine AMPPNP bound arrangement.<ref name="pept" /> For that reason having the Nϵ-BocLys positioned in this way it has the capability to participate in the hydrogen bonding with Asn346 amide group.<ref name="pept" /> This Asn346 is important when the amino acid is binding because it helps attach its carbonyl side chain; as well as the main-chain α-amino group to ensure the proper recognition it going to take place.<ref name="paper" /> From this Asn346 will also allow the substrate to effectively bind to the side chain amide group by inducible fitting the carbonyl group of the substrate into position.<ref name="pept" /> Next, the Cα-carbonyl groups of BocLys in turn will hydrogen bond Asn346 contrary to the α-amino group which is linked to α-phosphate group of AMPPNP.<ref name="pept" /> Additionally, the BocLys α-carboxyl group is directed to that it is associated outside from the active site allowing for the flexibility due to the ability to rotate around the Cɑ- Cβ bond.<ref name="pept" /> Furthermore, this active site contains an abundant of functional residues such as Lys192, Arg197, Arg217, Lys336, Lys435, Lys438 and Arg439 from the one domain and Arg310, Lys311 and Arg314 from the other, which participate in the effective binding with the tRNA.<ref name="paper" />

==Mechanism==

The proposed mechanism for the insertion of pyrrolysine into polypeptides initially begins with the activation of a special tRNA.<ref name="code"> PMID:12121639 </ref> This is completed by the charging of the 3' CCA end of tRNA as it interacts with lysine via aminoacylation by PyIRS in the presence of the exchange of ATP for AMP and PPi (inorganic pyrophosphate).<ref name="code" /> <ref name="paper" /> When ATP binds to PyIRS it causes a conformational change allowing this to happen.<ref name="paper" /> This will generate lysyl-tRNACUA which is then pre-translationally customized by the influence of the genes PyIB, PyIC and PyID generating Pyl-tRNACUA<ref name="code" /> This specific tRNAPyl is used to transport the amino acid pyrrolysine to the A-site located in the ribosome which is then added to the co-translated polypeptide chain.<ref name="code" /> To ensure the appropriate amino acid find its way to PyIRS, and not to any other class II aaRS present, PyIRS has special identification systems associated with it.<ref name="pept" /> These include special features such as its overall dimension, its structural layout and its binding ability to the hydrophibic active site.<ref name="pept" />
</StructureSection>

==3D structures of pyrrolysyl-tRNA synthetase==

[[pyrrolysyl-tRNA synthetase 3D structures]]

See [[Aminoacyl tRNA Synthetase]]

==Additional Resources==
For Additional information, see: [[Translation]] 

=References=
<references/>

[[Category:Topic Page]]

Pyrrolysyl-tRNA synthetase

2026-08-25T08:12:52Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='Sandbox_166/Scene_2/1' caption='Pyrrolysyl-tRNA synthetase complex with ATP analog and tert-butoxycarbo-lysine (PDB code [[2zin]])'>
__TOC__
== Function ==
[[Pyrrolysyl-tRNA synthetase]] (PyIRS) or '''Pyrrolysyl-tRNA ligase''' is encoded by the gene pyIS and is found to belong as a part of the group of enzymatic proteins whose role involves the cellular process of tRNA aminoacylation required for protein translation.<ref name="trans"> PMID:17267409 </ref> In particular, PyIRS is required for the activation of the amino acid [[Pyrrolysine]] as it associates with a tRNA generating a specific tRNAPyl, which is then further used to transfer the amino acid to a growing polypeptide.<ref name="pept"> PMID:19022179 </ref> The involvement of PyIRS is carried out due to the anticodon CUA on the suppressor tRNAPyl that is complementary to the UAG codon.<ref name="amber"> PMID:1796745 </ref> <ref>PMID:15314242 </ref> The interesting fact is that this is done by the response of the codon UAG (amber codon) on the mRNA that is normally a stop codon in other organisms. Pyrrolysine (Pyl) is the 22nd existing amino acid genetically encoded in nature that was first discovered as a byproduct contained by the active site of monomethylamine methyltransferase, exclusively from Methanosarcina barkeri (M. barkeri) species.<ref name="pept" /> <ref name="barkeri"> PMID:19118381 </ref> Thus, it is utilized by a variety of organisms that metabolize methylamines for acquiring energy such as methanogenic Archaea of the family Methanosarcinace; along with two known bacterium species<ref name="trans" /> <ref name="barkeri" /> Pyrrolysine’s structural makeup consists of 4-methylpyrroline-5-carboxylate in amide linkage with the Nϵ of lysine.<ref name="lysine">PMID:16096277 </ref> This arrangement is comparable to lysine; however, being its derivative it contains an added pyrroline ring that is found to lie situated at the back of the structure.<ref name="lysine" />

In addition, by observing M. barkeri cellular mechanisms containing PyIRS it was detected that it furthermore has the capability to activate an assortment of other imitative of pyrrolysine/lysine; as well as amino acids that are non-canonical.<ref>PMID:17126325 </ref> These amino acids can then be further added to their specialized tRNAPyl; inventing new polypeptides.<ref name="barkeri" /> This procedure is performed by extracting PyIRS, and the amber suppressor tRNAPyl from Methanosarcina. When obtained it must be ensured that the PyIRS-tRNAPyl pair are going to perform their specific roles with the selected amino acids to produce polypeptides containing them.<ref name="amber" /> Thus, their structural components are manipulated and then experimentally designed for the recognition and for the unique aminoacylation intended for it.<ref name="amber" /> Once this has been completed it then is carefully placed into a bacterium species such as Escherichia coli (E. coli).<ref name="amber" /> The reason that this is successful is because once inserted tRNAPyl function as an orthogonal pair with aaRS-tRNA that will not interfere with cellular mechanisms and other components of translation.<ref name="pept" /> <ref name="amber" /> Some of the lysine derivatives such as AcLys, ZLys, BocLys, AlocLys and AzZLys have been experimentally trialed and as a result, have been successfully translated into proteins.<ref name="amber" /> In particular interest, Nϵ-(tert-butyloxycarbonyl –L-lysine (BocLys) is a non-natural amino acid that is a deviation from the structure of lysine which can be intergraded into polypeptides utilizing the amber codon by the process of being esterified to tRNAPyl by PyIRS in E.coli for the incorporation into proteins.<ref name="pept" /> By using this method we can obtain proteins with manipulated structures and functions that can serve useful purposes in studying cellular processes and in altering further mechanisms. See also [[Ligases]].

==Structure==
<scene name='Sandbox_166/2ndstructure/3'>Showing the chains and bound BocLys</scene> ([[2zin]]).
Pyrrolysyl-tRNA synthetase (PyIRS) catalytic complex attached with <scene name='Sandbox_166/2ndstructure/6'>BocLys</scene>, and along with adenosine 5’ (beta, gamma-imido) triphosphate (AMMPPNP) demonstrates the now known structural components and configuration that is needed for the efficient recognition of amino acids and the aminoacylation by PyIRS.<ref name="pept" /> As shown in figure 1, it consists of a multi domain polypeptide made of 1 chain (Chain A) comprising of a total length of 291 residues with 2 catalytic domains; PRK06253 and class_II_aaRS-like_core t.<ref name="pept" /> Furthermore, the structure is observed to consisting of 9 <scene name='Sandbox_166/2ndstructure/1'>α-helices</scene> (95 residues) making 32% of the structure, and the remaining is 12 <scene name='Sandbox_166/2ndstructure/2'>β-strands</scene> (59 residues) consisting of 20% of the other structure. In addition, its structure components require the presence of the 4 ligands; ANP, EDO, LBY, and MG for the protein to correctly perform its biological function.

PyIRS structure is found to enclose a hydrophobic interior where the catalytic activity of recognition and activation of the amino acids is going to take place.<ref name="paper"> PMID:18387634 </ref> This area creates a suitable environment for the binding to occur and for accommodating the residues of pyrrolysine methyl-pyrroline ring inside so it has the capability so further interact with the active-side residues available.<ref name="paper" /> It has been shown, that in order for the amino acid to successfully come in contact proper size of PyIRS must be incorporated at the Nϵ-carbonyl group.<ref name="pept" /> By using the Fo-Fc omit map and with the visible electron density in the active site it was experimentally trialed that the Nϵ-Boc group is situated in the hydrophobic interior in the similar was as the already observed traditional pyrrolysine AMPPNP bound arrangement.<ref name="pept" /> For that reason having the Nϵ-BocLys positioned in this way it has the capability to participate in the hydrogen bonding with Asn346 amide group.<ref name="pept" /> This Asn346 is important when the amino acid is binding because it helps attach its carbonyl side chain; as well as the main-chain α-amino group to ensure the proper recognition it going to take place.<ref name="paper" /> From this Asn346 will also allow the substrate to effectively bind to the side chain amide group by inducible fitting the carbonyl group of the substrate into position.<ref name="pept" /> Next, the Cα-carbonyl groups of BocLys in turn will hydrogen bond Asn346 contrary to the α-amino group which is linked to α-phosphate group of AMPPNP.<ref name="pept" /> Additionally, the BocLys α-carboxyl group is directed to that it is associated outside from the active site allowing for the flexibility due to the ability to rotate around the Cɑ- Cβ bond.<ref name="pept" /> Furthermore, this active site contains an abundant of functional residues such as Lys192, Arg197, Arg217, Lys336, Lys435, Lys438 and Arg439 from the one domain and Arg310, Lys311 and Arg314 from the other, which participate in the effective binding with the tRNA.<ref name="paper" />

==Mechanism==

The proposed mechanism for the insertion of pyrrolysine into polypeptides initially begins with the activation of a special tRNA.<ref name="code"> PMID:12121639 </ref> This is completed by the charging of the 3' CCA end of tRNA as it interacts with lysine via aminoacylation by PyIRS in the presence of the exchange of ATP for AMP and PPi (inorganic pyrophosphate).<ref name="code" /> <ref name="paper" /> When ATP binds to PyIRS it causes a conformational change allowing this to happen.<ref name="paper" /> This will generate lysyl-tRNACUA which is then pre-translationally customized by the influence of the genes PyIB, PyIC and PyID generating Pyl-tRNACUA<ref name="code" /> This specific tRNAPyl is used to transport the amino acid pyrrolysine to the A-site located in the ribosome which is then added to the co-translated polypeptide chain.<ref name="code" /> To ensure the appropriate amino acid find its way to PyIRS, and not to any other class II aaRS present, PyIRS has special identification systems associated with it.<ref name="pept" /> These include special features such as its overall dimension, its structural layout and its binding ability to the hydrophibic active site.<ref name="pept" />
</StructureSection>

==3D structures of pyrrolysyl-tRNA synthetase==

See [[Aminoacyl tRNA Synthetase]]

==Additional Resources==
For Additional information, see: [[Translation]] 

=References=
<references/>

[[Category:Topic Page]]

Proto-oncogene serine/threonine-protein kinase

2026-08-24T09:49:25Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='54/542285/Cv/1' caption='Pim-1 complex with consensus peptide, inhibitor and Cl- ion [[3cy2]]'>

== Function ==
'''Proto-oncogene serine/threonine-protein kinase''' are a subset of '''serine/threonine-protein kinase''' which upon mutating cause cancer development.
'''Proto-oncogene serine/threonine-protein kinase (Pim1)''' is the provirus integration site for Moloney murine leukemia virus 1<ref>PMID:15694833</ref>. Pim1 is involved in cell cycle progression, apoptosis, transcriptional activation and signalling pathways. Pim1 phosphorylates and inhibits proapoptotic proteins. For details see [[Student Project 6 for UMass Chemistry 423 Spring 2015]]. See also [[Oncogenes & Tumor Suppressor Genes]].
* '''b-Raf''' is related to retroviral oncogenes and participates in cellular signal transduction. B-Raf domains include the kinase domain - residues 444-721 and Ras-binding domain - residues 153-237. Mutated B-Raf was found in some human cancers<ref>PMID:12460918</ref>.
See more in [[B-RAF with PLX4032]]; [[Mitogen-activated protein kinase cascade]].

* '''c-Raf''' is part of the MAPK pathway. c-Raf domains include the kinase domain - residues 323-618, cysteine-rich domain – residues 136-187 and Ras-binding domain - residues 51-132. Mutations of c-Raf are possible causes of Noonan syndrome<ref>PMID:23737487</ref>. For details on '''c-Raf''' see [[Molecular Playground/C-Raf]] and [[Mitogen-activated protein kinase cascade]].
*'''a-RAF''' stabilizes B-RAF:C-RAF complexes and thus regulates cell signalling<ref>PMID:22926515</ref>.
*'''AKT1''' has a role in tumor progression<ref>PMID:38860522</ref>.
*'''AKT2''' is critical to control of glucose metabolism by insulin <ref>PMID:19883618</ref>.
*'''AKT3''' is required for biogenesis of mitochondria <ref>PMID:24081905</ref>.

== Relevance ==
Pim1 is a progression marker in diffuse large B-cell lymphoma<ref>PMID:22722314</ref>.

== Disease ==
Pim-1 plays a pivotal role in several tumor relevant signaling pathways and is relevant to colon carcinoma<ref>PMID:23814490</ref>.

== Structural highlights ==
Pim1 is phosphorylated on serine 261 (PSer). The <scene name='54/542285/Cv/4'>consensus peptide (pimtide) ARKRRRHPSGPPTA binds strongly to Pim1</scene><ref>PMID:22136433</ref>. Water molecules are shown as red spheres.

==pim-1 3D structures==

[[Proto-oncogene serine/threonine protein kinase 3D structures]]
</StructureSection>

== References ==
<references/>
[[Category:Topic Page]]

Serine/threonine protein kinase

2026-08-24T09:48:22Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='Journal:JBIC:2/Opening/1' caption='Crystal Structure of Glycogen Synthase Kinase 3ß bound to Anticancer Ruthenium Complex'>

__TOC__

== Function ==
* '''Serine/threonine protein kinase''' 1 ('''Chk1''') phosphorylates cdc25A, cdc25B and cdc25C. Upon phosphorylation, cdc25 binds adaptor protein and the cell is prevented from entering mitosis<ref>PMID:12781359</ref>. 
* [[Cyclin-dependent kinases]]
* '''Chk2 (Checkpoint kinase 2)''' phosphorylates cdc25C at Ser-216. 
* '''Chk6''' called also '''Aurora A''' is critical for the formation of mitotic spindles during cellular mitosis. Chk6 is phosphorylated at residues Thr287 and Thr288<ref>PMID:15501446</ref>. 
* '''Chk13 (Polo-like kinase 1 or Plk1)''' functions during the M phase of the cell cycle including the regulation of centrosome maturation and spindle assembly. Chk13 binds and phosphorylates proteins which are already phosphorylated on a motif recognized by its POLO-box domain (Pbd) at the C terminal. Human Chk13 contains catalytic domain (residues 13-345) and POLO-box domain (residues 345-603)<ref>PMID:15640844</ref>.

* '''Chk11''' see [[STK11]].

* '''Chk Pak''' see [[Student Project 1 for UMass Chemistry 423 Spring 2015]]<ref>PMID:19165420</ref>.

* '''[[Glycogen synthase kinase 3]]''' (GSK-3) is a serine/threonine protein kinase. GSK-3 is active in a number of intracellular signaling pathways. GSK-3 regulates glycogen synthase as well as other proteins. GSK-3 inhibition is studied as a therapeutic target in diseases like Alzheimer, diabetes, bipolar disorder and some cancers<ref>PMID:17530463</ref>.

* '''B-Raf''' is related to retroviral oncogenes and participates in cellular signal transduction. B-Raf domains include the kinase domain - residues 444-721 and Ras-binding domain - residues 153-237. Mutated B-Raf was found in some human cancers<ref>PMID:12460918</ref>.
See more in [[B-RAF with PLX4032]]; [[Mitogen-activated protein kinase cascade]].

* '''c-Raf''' is part of the MAPK pathway. c-Raf domains include the kinase domain - residues 323-618, cysteine-rich domain – residues 136-187 and Ras-binding domain - residues 51-132. Mutations of c-Raf are possible causes of Noonan syndrome<ref>PMID:23737487</ref>. For details on '''c-Raf''' see [[Molecular Playground/C-Raf]] and [[Mitogen-activated protein kinase cascade]]..

* '''mTOR''' (mammalian target of [[Rapamycin]]) integrates the input from insulin, growth factors and amino acids. [[Rapamycin]] inhibits mTOR by association with FKBP12<ref>PMID:22500797</ref>. See also [[PI3K/AKT/mTOR signaling pathway]].

* '''Gcn2''' (Generl Control Nonderepressible 2) senses amino acid deficiency by binding to uncharged tRNA<ref>PMID:26982722</ref>.

* '''PRK1''' or serine/threonine protein kinase N1 belongs th protein kinase C family. PRK1 may mediate the Rho-independent signaling pathway. For more details see [[Student Project 1 for UMass Chemistry 423 Spring 2015]].

*'''LRRK1, LRRK2 or leucine-rich repeat kinase''' phosphorylate Rab proteins <ref>PMID:33459343</ref>.
*'''RIP''' regulates apoptosis<ref>PMID:9529147</ref>.
*'''Ulk1, Ulk2''' play a role in activating autophagy in mammals<ref>PMID:18936157</ref>.
*'''Hipa''' phosphorylates Glu-tRNA synthetase causing bacterial antibiotic persistence <ref>PMID:24343429</ref>.

* '''Pim, a-RAF, b-RAF, c-RAF, AKT1, AKT2, AKT3 ''' see [[Proto-oncogene serine/threonine-protein kinase]]

*[[Leucine-rich repeat serine/threonine-protein kinase 2]] (LRRK2)

*Protein kinase B (PKB), also known as '''AKT''', is the collective name of a set of three serine/threonine-specific protein kinases that play key roles in multiple cellular processes such as glucose metabolism, apoptosis, cell proliferation, transcription, and cell migration. For example of AKT1 see [[3mv5]]. '''Rac-α''' or '''AKT1''' acts in cell growth and survival. '''Rac-β''' or '''AKT2''' acts in metabolism. '''Rac-γ''' or '''AKT3''' acts in the nervous system.

For details on '''Snf1-related kinase''' see 
*[[ABA-regulated SNRK2 Protein Kinase]] 
*[[ABA Signaling Pathway]].

*See also [[Receptor protein serine/threonine kinases]]

==Structure of Anticancer Ruthenium Half-Sandwich Complex Bound to Glycogen Synthase Kinase 3ß <ref>DOI 10.1007/s00775-010-0699-x</ref>==
        A crystal structure of an <scene name='Journal:JBIC:2/Half_sandwich_complex_no_bonds/1'>organometallic half-sandwich ruthenium complex </scene>bound to the protein kinase glycogen synthase kinase 3ß (GSK-3ß) has been determined and reveals that the inhibitor binds to the <scene name='Journal:JBIC:2/Atp_binding_site2/2'>ATP binding site</scene> via an induced fit mechanism utlizing several <scene name='Journal:JBIC:2/Half_sandwich_complex/3'>hydrogen bonds</scene> and <scene name='Journal:JBIC:2/Half_sandwich_hydrophobic_stic/1'>hydrophobic interactions</scene>. Importantly, the metal is not involved in any direct interaction with the protein kinase but fulfills a purely structural role. The unique, bulky molecular structure of the half-sandwich complex with the CO-ligand oriented perpendicular to the pyridocarbazole heterocycle allows the complex to stretch the whole distance <scene name='Journal:JBIC:2/Half_sandwich_hydrophobic/5'>sandwiched between the faces of the N- and C-terminal lobes</scene> and to interact tightly with <scene name='Journal:JBIC:2/Glycine_rich_loop2/4'>the flexible glycine-rich loop</scene>. Although this complex is a conventional ATP-competitive binder, the unique shape of the complex allows novel interactions with the glycine-rich loop which are crucial for binding potency and selectivity. It can be hypothesized that coordination spheres which present other ligands towards the glycine-rich loop might display completely different protein kinase selectivities.

==3D structures of serine/threonine protein kinase==
[[Serine/threonine protein kinase 3D structures]]

</StructureSection>

===References===
<references/>

[[Category:Topic Page]]

Proto-oncogene serine/threonine-protein kinase

2026-08-24T09:46:15Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='54/542285/Cv/1' caption='Pim-1 complex with consensus peptide, inhibitor and Cl- ion [[3cy2]]'>

== Function ==
'''Proto-oncogene serine/threonine-protein kinase''' are a subset of '''serine/threonine-protein kinase''' which upon mutating cause cancer development.
'''Proto-oncogene serine/threonine-protein kinase (Pim1)''' is the provirus integration site for Moloney murine leukemia virus 1<ref>PMID:15694833</ref>. Pim1 is involved in cell cycle progression, apoptosis, transcriptional activation and signalling pathways. Pim1 phosphorylates and inhibits proapoptotic proteins. For details see [[Student Project 6 for UMass Chemistry 423 Spring 2015]]. See also [[Oncogenes & Tumor Suppressor Genes]].
* '''b-Raf''' is related to retroviral oncogenes and participates in cellular signal transduction. B-Raf domains include the kinase domain - residues 444-721 and Ras-binding domain - residues 153-237. Mutated B-Raf was found in some human cancers<ref>PMID:12460918</ref>.
See more in [[B-RAF with PLX4032]]; [[Mitogen-activated protein kinase cascade]].

* '''c-Raf''' is part of the MAPK pathway. c-Raf domains include the kinase domain - residues 323-618, cysteine-rich domain – residues 136-187 and Ras-binding domain - residues 51-132. Mutations of c-Raf are possible causes of Noonan syndrome<ref>PMID:23737487</ref>. For details on '''c-Raf''' see [[Molecular Playground/C-Raf]] and [[Mitogen-activated protein kinase cascade]].
*'''a-RAF''' stabilizes B-RAF:C-RAF complexes and thus regulates cell signalling<ref>PMID:22926515</ref>.
*'''AKT1''' has a role in tumor progression<ref>PMID:38860522</ref>.
*'''AKT2''' is critical to control of glucose metabolism by insulin <ref>PMID:19883618</ref>.
*'''AKT3''' is required for biogenesis of mitochondria <ref>PMID:24081905</ref>.
*'''LRRK1, LRRK2 or leucine-rich repeat kinase''' phosphorylate Rab proteins <ref>PMID:33459343</ref>.
*'''RIP''' regulates apoptosis<ref>PMID:9529147</ref>.
*'''Ulk1, Ulk2''' play a role in activating autophagy in mammals<ref>PMID:18936157</ref>.
*'''Hipa''' phosphorylates Glu-tRNA synthetase causing bacterial antibiotic persistence <ref>PMID:24343429</ref>.

== Relevance ==
Pim1 is a progression marker in diffuse large B-cell lymphoma<ref>PMID:22722314</ref>.

== Disease ==
Pim-1 plays a pivotal role in several tumor relevant signaling pathways and is relevant to colon carcinoma<ref>PMID:23814490</ref>.

== Structural highlights ==
Pim1 is phosphorylated on serine 261 (PSer). The <scene name='54/542285/Cv/4'>consensus peptide (pimtide) ARKRRRHPSGPPTA binds strongly to Pim1</scene><ref>PMID:22136433</ref>. Water molecules are shown as red spheres.

==pim-1 3D structures==

[[Proto-oncogene serine/threonine protein kinase 3D structures]]
</StructureSection>

== References ==
<references/>
[[Category:Topic Page]]

Serine/threonine protein kinase

2026-08-24T09:44:32Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='Journal:JBIC:2/Opening/1' caption='Crystal Structure of Glycogen Synthase Kinase 3ß bound to Anticancer Ruthenium Complex'>

__TOC__

== Function ==
* '''Serine/threonine protein kinase''' 1 ('''Chk1''') phosphorylates cdc25A, cdc25B and cdc25C. Upon phosphorylation, cdc25 binds adaptor protein and the cell is prevented from entering mitosis<ref>PMID:12781359</ref>. 
* [[Cyclin-dependent kinases]]
* '''Chk2 (Checkpoint kinase 2)''' phosphorylates cdc25C at Ser-216. 
* '''Chk6''' called also '''Aurora A''' is critical for the formation of mitotic spindles during cellular mitosis. Chk6 is phosphorylated at residues Thr287 and Thr288<ref>PMID:15501446</ref>. 
* '''Chk13 (Polo-like kinase 1 or Plk1)''' functions during the M phase of the cell cycle including the regulation of centrosome maturation and spindle assembly. Chk13 binds and phosphorylates proteins which are already phosphorylated on a motif recognized by its POLO-box domain (Pbd) at the C terminal. Human Chk13 contains catalytic domain (residues 13-345) and POLO-box domain (residues 345-603)<ref>PMID:15640844</ref>.

* '''Chk11''' see [[STK11]].

* '''Chk Pak''' see [[Student Project 1 for UMass Chemistry 423 Spring 2015]]<ref>PMID:19165420</ref>.

* '''[[Glycogen synthase kinase 3]]''' (GSK-3) is a serine/threonine protein kinase. GSK-3 is active in a number of intracellular signaling pathways. GSK-3 regulates glycogen synthase as well as other proteins. GSK-3 inhibition is studied as a therapeutic target in diseases like Alzheimer, diabetes, bipolar disorder and some cancers<ref>PMID:17530463</ref>.

* '''B-Raf''' is related to retroviral oncogenes and participates in cellular signal transduction. B-Raf domains include the kinase domain - residues 444-721 and Ras-binding domain - residues 153-237. Mutated B-Raf was found in some human cancers<ref>PMID:12460918</ref>.
See more in [[B-RAF with PLX4032]]; [[Mitogen-activated protein kinase cascade]].

* '''c-Raf''' is part of the MAPK pathway. c-Raf domains include the kinase domain - residues 323-618, cysteine-rich domain – residues 136-187 and Ras-binding domain - residues 51-132. Mutations of c-Raf are possible causes of Noonan syndrome<ref>PMID:23737487</ref>. For details on '''c-Raf''' see [[Molecular Playground/C-Raf]] and [[Mitogen-activated protein kinase cascade]]..

* '''mTOR''' (mammalian target of [[Rapamycin]]) integrates the input from insulin, growth factors and amino acids. [[Rapamycin]] inhibits mTOR by association with FKBP12<ref>PMID:22500797</ref>. See also [[PI3K/AKT/mTOR signaling pathway]].

* '''Gcn2''' (Generl Control Nonderepressible 2) senses amino acid deficiency by binding to uncharged tRNA<ref>PMID:26982722</ref>.

* '''PRK1''' or serine/threonine protein kinase N1 belongs th protein kinase C family. PRK1 may mediate the Rho-independent signaling pathway. For more details see [[Student Project 1 for UMass Chemistry 423 Spring 2015]].

* '''Pim, a-RAF, b-RAF, c-RAF, AKT1, AKT2, AKT3 ''' see [[Proto-oncogene serine/threonine-protein kinase]]

*[[Leucine-rich repeat serine/threonine-protein kinase 2]] (LRRK2)

*Protein kinase B (PKB), also known as '''AKT''', is the collective name of a set of three serine/threonine-specific protein kinases that play key roles in multiple cellular processes such as glucose metabolism, apoptosis, cell proliferation, transcription, and cell migration. For example of AKT1 see [[3mv5]]. '''Rac-α''' or '''AKT1''' acts in cell growth and survival. '''Rac-β''' or '''AKT2''' acts in metabolism. '''Rac-γ''' or '''AKT3''' acts in the nervous system.

For details on '''Snf1-related kinase''' see 
*[[ABA-regulated SNRK2 Protein Kinase]] 
*[[ABA Signaling Pathway]].

*See also [[Receptor protein serine/threonine kinases]]

==Structure of Anticancer Ruthenium Half-Sandwich Complex Bound to Glycogen Synthase Kinase 3ß <ref>DOI 10.1007/s00775-010-0699-x</ref>==
        A crystal structure of an <scene name='Journal:JBIC:2/Half_sandwich_complex_no_bonds/1'>organometallic half-sandwich ruthenium complex </scene>bound to the protein kinase glycogen synthase kinase 3ß (GSK-3ß) has been determined and reveals that the inhibitor binds to the <scene name='Journal:JBIC:2/Atp_binding_site2/2'>ATP binding site</scene> via an induced fit mechanism utlizing several <scene name='Journal:JBIC:2/Half_sandwich_complex/3'>hydrogen bonds</scene> and <scene name='Journal:JBIC:2/Half_sandwich_hydrophobic_stic/1'>hydrophobic interactions</scene>. Importantly, the metal is not involved in any direct interaction with the protein kinase but fulfills a purely structural role. The unique, bulky molecular structure of the half-sandwich complex with the CO-ligand oriented perpendicular to the pyridocarbazole heterocycle allows the complex to stretch the whole distance <scene name='Journal:JBIC:2/Half_sandwich_hydrophobic/5'>sandwiched between the faces of the N- and C-terminal lobes</scene> and to interact tightly with <scene name='Journal:JBIC:2/Glycine_rich_loop2/4'>the flexible glycine-rich loop</scene>. Although this complex is a conventional ATP-competitive binder, the unique shape of the complex allows novel interactions with the glycine-rich loop which are crucial for binding potency and selectivity. It can be hypothesized that coordination spheres which present other ligands towards the glycine-rich loop might display completely different protein kinase selectivities.

==3D structures of serine/threonine protein kinase==
[[Serine/threonine protein kinase 3D structures]]

</StructureSection>

===References===
<references/>

[[Category:Topic Page]]

Proto-oncogene serine/threonine protein kinase 3D structures

2026-08-24T09:31:24Z

Michal Harel: Created page with "Proto-oncogene serine/threonine protein kinase Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} {{#tree:id=OrganizedByTopic|openlevels=0| *'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123;kinase 144-480 **1unp, 1unr – Rac-α hChk pleckstrin homology domain **1h10, 1unq, 2uvm – hRac-α hChk pleckstrin homology..."

Proto-oncogene serine/threonine protein kinase

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123;kinase 144-480

**[[1unp]], [[1unr]] – Rac-α hChk pleckstrin homology domain 
**[[1h10]], [[1unq]], [[2uvm]] – hRac-α hChk pleckstrin homology domain + inositol tetrakisphosphate 
**[[3o96]], [[4ejn]], [[6hhf]], [[6hhg]], [[6hhh]], [[6hhi]], [[6hhj]], [[6s9w]], [[6s9x]] - hRac-α hChk + inhibitor 
**[[5kcv]], [[7nh4]], [[7nh5]] - hRac-α hChk (mutant) + inhibitor 
**[[4ekl]], [[4gv1]] - hRac-α hChk kinase domain + inhibitor 
**[[3qkm]], [[6ccy]] - hRac-α hChk kinase domain (mutant) + inhibitor 
**[[6buu]] - hRac-α hChk kinase domain + bisubstrate peptide 
**[[4ekk]] - hRac-α hChk kinase domain (mutant) + GSK3 peptide + AMPPNP 
**[[6npz]] - hRac-α hChk kinase domain + peptide + inhibitor 
**[[3ow4]], [[3qkk]], [[3qkl]], [[6buu]] - hRac-α hChk kinase domain (mutant) + peptide + inhibitor 
**[[7apj]] - hRac-α hChk + nanobody 

*'''Rac-β hChk (AKT2)'''

**[[1gzk]], [[1gzn]], [[1gzo]], [[1mrv]], [[1mry]] – hRac-β hChk kinase domain 
**[[1p6s]] - hRac-β hChk pleckstrin homology domain - NMR 
**[[1o6k]] - hRac-β hChk kinase domain + GSK3 peptide + AMPPNP 
**[[2jdo]], [[2jdr]], [[2uw9]], [[2x39]], [[3cqu]], [[3cqw]] - hRac-β hChk kinase domain + GSK3 peptide + inhibitor 
**[[3e87]], [[3e88]], [[3e8d]] - Rac-β hChk kinase domain (mutant) + GSK3 peptide + inhibitor 
**[[3d0e]], [[8q61]] - hRac-β hChk kinase domain (mutant) + inhibitor 

*'''Rac-γ hChk (ATK3)'''

**[[2x18]] – Rac-γ hChk PH domain 

*'''A-Raf'''

**[[1wxm]] – hA-Raf RAS-binding domain 19-91 - NMR 
**[[2mse]] – hA-Raf RAS-binding domain + APOA-I + K-ras - NMR 

*'''B-Raf'''; domains - BRS 38-116; Ras-binding 153-237; kinase 445-723

**[[8dgs]], [[8dgt]] – hB-Raf in Ras/Raf complex – Cryo EM 
**[[7z37]], [[7z38]], [[7zr5]] – hB-Raf + Hsp90 + CDC37 + PP5 – Cryo EM 
**[[1uwh]], [[3c4c]], [[6v2u]], [[6xfp]], [[6xlo]], [[8f7o]], [[8f7p]] – hB-Raf kinase domain + anticancer drug 
**[[1uwj]], [[6p3d]] – hB-Raf kinase domain (mutant) + anticancer drug 
**[[2fb8]], [[3d4q]], [[3e26]], [[3ii5]], [[3ppj]], [[3ppk]], [[3prf]], [[3pri]], [[3psb]], [[3psd]], [[3q4c]], [[3q96]], [[3skc]], [[3tv4]], [[3tv6]], [[4dbn]], [[4e26]], [[4e4x]], [[4ehe]], [[4fc0]], [[4g9c]], [[4h58]], [[4ksp]], [[4ksq]], [[4mbj]], [[4pp7]], [[6cad]], [[7shv]] – hB-Raf kinase domain + pyrazole inhibitor 
**[[3idp]], [[4ehg]], [[4fk3]], [[4g9r]], [[4jvg]], [[4mnf]], [[4r5y]], [[4rzv]], [[4rzw]], [[4wo5]], [[4xv1]], [[4xv2]], [[4xv3]], [[4xv9]], [[4yht]], [[5c9c]], [[5hi2]], [[5ita]], [[5jrq]], [[5jsm]], [[5jt2]], [[6nsq]], [[6p7d]], [[6uuo]] – hB-Raf kinase domain (mutant) + pyrazole inhibitor 
**[[5csw]], [[5csx]], [[5ct7]], [[5fd2]], [[5hid]], [[5hie]], [[5val]], [[5vam]], [[6b8u]], [[6n0p]], [[6n0q]], [[7k0v]], [[7p3b]], [[7p3v]], [[8c7x]], [[8c7y]] - hB-Raf kinaseqdomain + inhibitor 
**[[6v34]] – hB-Raf kinase domain (mutant) + inhibitor 
**[[4mne]] – hB-Raf kinase domain + MAPKK1 
**[[8f7o]] – hB-Raf kinase domain + drug 
**[[7m0u]] – hB-Raf kinase domain + AMPPNP + drug 
**[[6u2h]] – hB-Raf kinase domain + 14-3-3 ζ/δ 
**[[7mfe]] – hB-Raf + 14-3-3 ζ/δ – Cryo EM 
**[[7mff]] – hB-Raf + 14-3-3 ζ/δ + inhibitor – Cryo EM 
**[[7mfd]] – hB-Raf + 14-3-3 ζ/δ + MEK + inhibitor – Cryo EM 
**[[6pp9]] – hB-Raf kinase domain + MEK1 + ANP 
**[[7m0x]], [[7m0z]] – hB-Raf kinase domain + MEK1 + ANP + inhibitor 
**[[7m0t]], [[7m0u]], [[7m0v]], [[7m0w]], [[7m0y]] – hB-Raf kinase domain + MEK1 + ANP + drug 
**[[6u2g]] – hB-Raf kinase domain + MEK1 + AMPPCP 
**[[5vr3]] – hB-Raf BRS domain 
**[[7jhp]] – hB-Raf BRS domain + Hras 
**[[6ntc]], [[6ntd]] – hB-Raf BRS domain (mutant) + Hras 
**[[6xi7]] – hB-Raf 52-188 + Kras 
**[[2l05]], [[5j17]], [[5j2r]] – hB-Raf RAS-binding domain - NMR 
**[[3ny5]] – hB-Raf RAS-binding domain 
**[[5j18]] – hB-Raf RAS-binding domain + inhibitor - NMR 
**[[6pts]], [[6ptw]] – hB-Raf 56-187 + Kras + apolipoprotein + GMPPNP - NMR 
**[[6q0k]], [[6uan]] – hB-Raf + 14-3-3 ζ – Cryo EM 
**[[6nyb]] – hB-Raf + 14-3-3 ζ + MEK1 – Cryo EM 
**[[6q0j]], [[6q0t]] – hB-Raf (mutant) + 14-3-3 ζ + MEK1 – Cryo EM 

*'''c-Raf'''; Domains – RAS-binding (RBD) 55-132; Cys-rich 136-187 (CBD); kinase 323-618

**[[1rfa]], [[8jna]], [[8jof]], [[8jog]] – hc-Raf RBD - NMR 
**[[1faq]], [[1far]] – hc-Raf cysteine-rich domain - NMR 
**[[3omv]] – hc-Raf kinase domain 
**[[1rrb]] – c-Raf RBD – NMR - rat 

*c-Raf complex with protein

**[[8cpd]] – hc-Raf + 14-3-3 protein zeta – Cryo EM 
**[[9mmp]] – hc-Raf + MEK1 + 14-3-3 protein zeta – Cryo EM 
**[[9mmr]] – hc-Raf (mutant) + MEK1 + 14-3-3 protein zeta – Cryo EM 
**[[1c1y]] – hc-Raf RBD + RAP1A 
**[[3kuc]] – hc-Raf RBD (mutant) + RAP1A 
**[[1gua]] – hc-Raf RBD + RAP1A + GPPNHP 
**[[8jnb]] – hc-Raf RBD + ligand 
**[[4g0n]], [[4g3x]] – hc-Raf RBD + GTPase Hras 
**[[3kud]] – hc-Raf RBD (mutant) + GTPase Hras 
**[[8epw]], [[8t74]] – hc-Raf RBD + GTPase K-ras 
**[[8t75]], [[9ygs]] – hc-Raf RBD-CRD + GTPase K-ras + GMPPNP 
**[[9ay7]], [[9aya]] – hc-Raf + MEK1 
**[[9mmq]] – hc-Raf + MEK1 – Cryo EM 
**[[9mms]] – hc-Raf (mutant) + MEK1 – Cryo EM 
**[[9o0u]], [[9o0v]] – hc-Raf (mutant) + MEK1 + ANP + inhibitor– Cryo EM 
**[[8u1l]] – hc-Raf + Hsp90 + CDC37 – Cryo EM 
**[[8gae]], [[8gft]] – hc-Raf + Hsp90 + CDC37 + PP5 – Cryo EM 

*Pim1 catalytic domain residues 14-313

**[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain 
**[[1yxs]] – hPim1 catalytic domain (mutant) 
**[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP 
**[[1yxu]] – hPim1 catalytic domain + AMP 
**[[1yxv]], [[5ipj]] – hPim1 catalytic domain + quinoline derivative 
**[[1yxx]] – hPim1 catalytic domain + indole derivative 
**[[2bzh]], [[2bzi]], [[2bzj]] – hPim1 catalytic domain (mutant) + organometallic ligand 
**[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3c4e]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umw]], [[3umx]], [[4enx]], [[4eny]], [[4k0y]], [[4k18]], [[4k1b]], [[4i41]], [[4iaa]], [[4ll5]], [[4lm5]], [[4lmu]], [[4mbi]], [[4mbl]], [[4med]], [[4mta]], [[4n6y]], [[4n6z]], [[4n70]], [[4xh6]], [[5iis]], [[5kgd]], [[5kge]], [[5kgg]], [[5kgi]], [[5kgk]], [[5kzi]], [[5vua]], [[5vub]], [[5vuc]], [[6mt0]], [[6vrv]], [[7oov]], [[7oow]], [[7oox]], [[7xsv]] – hPim1 catalytic domain + inhibitor 
**[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor 

*Pim1 kinase domain residues 92-404

**[[4jx3]] – hPim1 kinase domain 
**[[3uix]], [[5c1q]] – hPim1 kinase domain residues 120-404 + quinoline derivative 
**[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate 
**[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand 
**[[1xws]], [[4alu]], [[4alv]], [[4alw]], [[4as0]], [[4bzn]], [[4bzo]], [[4dtk]], [[4jx7]], [[4rbl]], [[4rc2]], [[4rc3]], [[4rc4]], [[4ty1]], [[4wrs]], [[4wsy]], [[4wt6]], [[4xhk]], [[5dgz]], [[5dhj]], [[5dia]], [[5dwr]], [[5eol]], [[5kcx]], [[5o11]], [[5o12]], [[5o13]], [[5tel]], [[5tex]], [[5toe]], [[5v80]], [[5v82]]. [[6bsk]], [[6kzi]], [[6l11]], [[6l12]], [[6l13]], [[6l14]], [[6l15]], [[6l16]], [[6l17]], [[6no8]], [[6no9]], [[6vru]], [[6ykd]], [[7zun]] – hPim1 kinase domain + inhibitor 
**[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor 

*Pim1 full length

**[[4rpv]], [[5tur]] - hPim1 + inhibitor 

*Pim1 complex with consensus peptide (pimtide)

**[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]], [[6qxk]] – hPim1 kinase domain + inhibitor + consensus peptide 
**[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide 
**[[2c3i]], [[5mzl]], [[5n4n]], [[5n4o]], [[5n4r]], [[5n4u]], [[5n4v]], [[5n4x]], [[5n4y]], [[5n4z]], [[5n50]], [[5n51]], [[5n52]], [[5n5l]], [[5n5m]], [[5ndt]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide 
**[[4gw8]], [[7qb2]], [[7qfm]], [[7z6u]], [[8afr]] – hPim1 catalytic domain (mutant) + inhibitor + pimtide 
**[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide 
**[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide 

*Pim1 containing phosphorylated Ser 261

**[[1yhs]] – hPim1 kinase domain + PSer + staurosporine 
**[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor 
**[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor 
**[[1yi4]] – hPim1 kinase domain + PSer + adenosine 

*Pim2

**[[4x7q]] – hPim2 catalytic domain + inhibitor 
**[[2iwi]] – hPim2 catalytic domain + Ru ligand 

}}
[[Category:Topic Page]]

Proto-oncogene serine/threonine-protein kinase

2026-08-24T09:28:51Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='54/542285/Cv/1' caption='Pim-1 complex with consensus peptide, inhibitor and Cl- ion [[3cy2]]'>

== Function ==
'''Proto-oncogene serine/threonine-protein kinase''' are a subset of '''serine/threonine-protein kinase''' which upon mutating cause cancer development.
'''Proto-oncogene serine/threonine-protein kinase (Pim1)''' is the provirus integration site for Moloney murine leukemia virus 1<ref>PMID:15694833</ref>. Pim1 is involved in cell cycle progression, apoptosis, transcriptional activation and signalling pathways. Pim1 phosphorylates and inhibits proapoptotic proteins. For details see [[Student Project 6 for UMass Chemistry 423 Spring 2015]]. See also [[Oncogenes & Tumor Suppressor Genes]].
*'''C-RAF''' regulates cell proliferation, cell death and metabolism<ref>PMID:29499332</ref>.
*'''B-RAF''' is mutated in ca. 7% of human cancers <ref>PMID:15279791</ref>.
*'''A-RAF''' stabilizes B-RAF:C-RAF complexes and thus regulates cell signalling<ref>PMID:22926515</ref>.
*'''AKT1''' has a role in tumor progression<ref>PMID:38860522</ref>.
*'''AKT2''' is critical to control of glucose metabolism by insulin <ref>PMID:19883618</ref>.
*'''AKT3''' is required for biogenesis of mitochondria <ref>PMID:24081905</ref>.
*'''LRRK1, LRRK2 or leucine-rich repeat kinase''' phosphorylate Rab proteins <ref>PMID:33459343</ref>.
*'''RIP''' regulates apoptosis<ref>PMID:9529147</ref>.
*'''Ulk1, Ulk2''' play a role in activating autophagy in mammals<ref>PMID:18936157</ref>.
*'''Hipa''' phosphorylates Glu-tRNA synthetase causing bacterial antibiotic persistence <ref>PMID:24343429</ref>.

== Relevance ==
Pim1 is a progression marker in diffuse large B-cell lymphoma<ref>PMID:22722314</ref>.

== Disease ==
Pim-1 plays a pivotal role in several tumor relevant signaling pathways and is relevant to colon carcinoma<ref>PMID:23814490</ref>.

== Structural highlights ==
Pim1 is phosphorylated on serine 261 (PSer). The <scene name='54/542285/Cv/4'>consensus peptide (pimtide) ARKRRRHPSGPPTA binds strongly to Pim1</scene><ref>PMID:22136433</ref>. Water molecules are shown as red spheres.

==pim-1 3D structures==

[[Proto-oncogene serine/threonine protein kinase 3D structures]]
</StructureSection>

== References ==
<references/>
[[Category:Topic Page]]

Proto-oncogene serine/threonine-protein kinase

2026-08-24T08:55:56Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='54/542285/Cv/1' caption='Pim-1 complex with consensus peptide, inhibitor and Cl- ion [[3cy2]]'>

== Function ==
'''Proto-oncogene serine/threonine-protein kinase (Pim1)''' is the provirus integration site for Moloney murine leukemia virus 1<ref>PMID:15694833</ref>. Pim1 is involved in cell cycle progression, apoptosis, transcriptional activation and signaling pathways. Pim1 phosphorylates and inhibits proapoptotic proteins. For details see [[Student Project 6 for UMass Chemistry 423 Spring 2015]]. See also [[Oncogenes & Tumor Suppressor Genes]].
*'''Chk1 or checkpoint kinase 1''' phosphorylates variety of proteins resulting in activation of DNA damage checkpoint and more<ref>PMID:23508805</ref>.
*'''Chk2 or checkpoint kinase 2''' has a role in cell cycle arrest and apoptosis by DNA damage <ref>PMID:15279791</ref>.
*'''Plk1 or Polo-like kinase 1''' phosphorylates variety of proteins affecting cell entry into mitosis, centrosome maturation, spindle assembly and cytokinesis<ref>PMID:34454931</ref>.
*'''Plk3 or Polo-like kinase 3''' becomes phosphorylated after DNA damage or mitotic spindle disruption <ref>PMID:12242661</ref>.
*'''Haspin''' phosphorylates histone H3 and thus affects mitosis <ref>PMID:28413956</ref>.
*'''mTOR or mechanistic target of rapamycin''' signaling influences longevity and aging <ref>PMID:29190625</ref>.
*'''LRRK1, LRRK2 or leucine-rich repeat kinase''' phosphorylate Rab proteins <ref>PMID:33459343</ref>.
*'''RIP''' regulates apoptosis<ref>PMID:9529147</ref>.
*'''Ulk1, Ulk2''' play a role in activating autophagy in mammals<ref>PMID:18936157</ref>.
*'''Hipa''' phosphorylates Glu-tRNA synthetase causing bacterial antibiotic persistence <ref>PMID:24343429</ref>.

== Relevance ==
Pim1 is a progression marker in diffuse large B-cell lymphoma<ref>PMID:22722314</ref>.

== Disease ==
Pim-1 plays a pivotal role in several tumor relevant signaling pathways and is relevant to colon carcinoma<ref>PMID:23814490</ref>.

== Structural highlights ==
Pim1 is phosphorylated on serine 261 (PSer). The <scene name='54/542285/Cv/4'>consensus peptide (pimtide) ARKRRRHPSGPPTA binds strongly to Pim1</scene><ref>PMID:22136433</ref>. Water molecules are shown as red spheres.

==pim-1 3D structures==

[[Proto-oncogene serine/threonine protein kinase 3D structures]]
</StructureSection>

== References ==
<references/>
[[Category:Topic Page]]

Pyrroline-5-carboxylate reductase

2026-08-24T07:28:52Z

Michal Harel:

<StructureSection load='2gr9' size='350' side='right' caption='Human pyrroline-5-carboxylate reductase complex with cofactor NADH and glutamate (PDB entry [[2gr9]])' scene=''>
== Function ==
'''Pyrroline-5-carboxylate reductase''' (PYCR) catalyzes the reversible oxidation of 1-pyrroline-5-carboxylate to proline using NAD or NADP as cofactors. This is the last step in the biosynthesis of proline from glutamate<ref>PMID:24467670</ref>.

== Disease ==
Mutations in PYCR cause microcephaly and hypomyelination<ref>PMID:25865492</ref>.

== Structural highlights ==
The active site of PYCR contains the NAD cofactor and glutamate<ref>PMID:16730026</ref>
</StructureSection>

==3D structures of pyrroline-5-carboxylate reductase==
{{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyrroline-5-carboxylate reductase

**[[2ger]] - hPYCR1 – human 
**[[6lhm]] – hPYCR2 
**[[5bse]] - bmPYCR - barrel medic 
**[[1yqg]] - NmPYCR – ''Neisseria meningitidis'' 
**[[2amf]] - SpPYCR – ''Streptococcus pyogenes'' 
**[[3gt0]] - PYCR – ''Bacillus cereus'' 

*Pyrroline-5-carboxylate reductase complex

**[[2izz]] – hPYCR1 + NAD 
**[[2gra]], [[5uat]], [[5uaw]], [[5uax]] – hPYCR1 + NADP 
**[[8dkg]] – hPYCR1 (mutant) + NAD 
**[[2gr9]] – hPYCR1 + glutamate + NAD 
**[[5uau]], [[6xp0]] – hPYCR1 + proline derivative 
**[[8vre]] – hPYCR1 + proline derivative + NAD 
**[[9rzz]] – hPYCR1 + pyrrolidine derivative 
**[[6xoz]], [[6xp1]], [[6xp2]], [[8tcu]], [[8tcv]], [[8tcw]], [[8tcx]], [[8tcy]], [[8tcz]], [[8td0]], [[8td1]], [[8td2]], [[8td3]], [[8td4]], [[8td5]], [[8td6]], [[8td7]], [[8td8]], [[8td9]], [[8tdb]], [[8tdc]], [[8tdd]], [[9p0q]], [[9p0r]], [[9p0s]], [[9p0t]], [[9p0u]], [[9p0v]], [[9s01]], [[9s02]], [[9s04]] – hPYCR1 + inhibitor 
**[[6xp3]] – hPYCR1 + carboxylic acid 
**[[9q45]] – hPYCR1 + inhibitor + NAD + carboxylate derivative 
**[[9q46]] – hPYCR1 + inhibitor + butyrate derivative 
**[[5uav]] – hPYCRt1 + tetrahydrofuroic acid + NADP 
**[[9q6g]] – hPYCR2 + inhibitor + NAD 
**[[5bsf]] - bmPYCR + NAD 
**[[5bsg]] - bmPYCR + NADP 
**[[5bsh]] - bmPYCR + proline 
**[[2ag8]] – NmPYCR + NADP 
**[[2ahr]] - SpPYCR + NADP 
**[[2rcy]] - PYCR + NADP – ''Plasmodium falciparum'' 
**[[3tri]] - PYCR + NADP – ''Coxiella burnetii'' 

}}
== References ==
<references/>
[[Category: Topic Page]]

Pyruvate carboxylase 3D structures

2026-08-23T10:03:32Z

Michal Harel:

==3D structures of pyruvate carboxylase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyruvate carboxylase; Domains – biotin carboxylase 1-461; carboxyltransferase (CT) 465-end

**[[7wta]], [[8hwl]], [[8j7o]] – hPC – human – Cryo EM 
**[[3bg9]] - hPC CT domain 
**[[3tw7]] – RePC – Rhizobium etli 
**[[4jx4]] – RePC CT domain 
**[[1ulz]] – PC biotin carboxylase domain (mutant) – Aquifex aeolicus 
**[[2dzd]] – PC biotin carboxylase domain – Geobacillus thermodenitrificans 
**[[4qsl]] – LmPC – Listeria monocytogenes 
**[[7zz0]] - LlPC – Lactococcus lactis – Cryo EM 
**[[5ks8]] – PC subunit a+b – Methylobacillus flagellatus 
**[[9vmh]], [[9vvk]] – MtPC – Mycobactrium tuberculosis – Cryo EM 
**[[9ueq]] - MtPC CT domain 

*Pyruvate carboxylase binary complex

**[[7wtc]] - hPC + acetyl-CoA – Cryo EM 
**[[3bg3]] - hPC CT domain + pyruvate 
**[[7zyz]] - LlPC + oxaloacetate – Cryo EM 
**[[7zz5]] - LlPC + acetyl-CoA – Cryo EM 
**[[7zz2]], [[7zz6]] - LlPC + pyruvate – Cryo EM 
**[[5vyw]] - LlPC + biotin 
**[[3hb9]], [[3hbl]], [[4hnu]] - SaPC (mutant) + ADP – Staphlococcus aureus 
**[[4qsh]], [[4qsk]] - LmPC + cAMP 
**[[4mfd]] - RePC CT domain + oxalate 
**[[4mim]] - RePC CT domain + pyruvate derivative 

*Pyruvate carboxylase ternary complex

**[[8xl9]] - hPC + biotin – Cryo EM 
**[[7wtb]], [[7wte]] - hPC + acetyl-CoA + ANP – Cryo EM 
**[[7wtd]], [[7zz4]] - LlPC + acetyl-CoA + ATP – Cryo EM 
**[[9ubg]] - LlPC + acetyl-CoA + ADP – Cryo EM 
**[[5vyz]], [[5vz0]] - LlPC + ADP + cAMP 
**[[7zz1]] - LlPC + biotin + oxaloacetate – Cryo EM 
**[[4jx5]] – RePC CT domain + pyruvate 
**[[4jx6]] – RePC CT domain (mutant) + pyruvate 
**[[4m6v]] – RePC CT domain + pyruvate + biocytin 
**[[4mfe]] – RePC CT domain + pyruvate derivative + biotin 
**[[2qf7]] - RePC + acetyl-CoA + AGS 
**[[3tw6]] - RePC (mutant) + acetyl-CoA + ADP 
**[[4loc]] - RePC + biotin + oxamate 
**[[4hnt]], [[4hnv]] - SaPC (mutant) + ADP + ATP 
**[[3ho8]], [[8gk8]] - SaPC + acetyl-CoA + imidazole derivative 

*Pyruvate carboxylase higher complex

**[[7zyy]] - LlPC + acetyl-CoA + ATP + pyruvate – Cryo EM 
**[[7zz8]] - LlPC + acetyl-CoA + ADP + cAMP + pyruvate – Cryo EM 
**[[7zz3]] - LlPC + acetyl-CoA + ADP + biotin + pyruvate – Cryo EM 
**[[3bg5]] - SaPC + pyruvate+ imidazole derivative + ATP 

}}
[[Category:Topic Page]]

Pyrroline-5-carboxylate dehydrogenase

2026-08-23T08:36:45Z

Michal Harel:

<StructureSection load='' size='350' side='right' caption='Mouse pyrroline-5-carboxylate dehydrogenase dimer complex with glutarate and PEG400 (PDB entry [[4lh3]])' scene='51/510199/Cv1/1'>
== Function ==
'''Pyrroline-5-carboxylate dehydrogenase''' or '''Delta-1-pyrroline-5-carboxylate dehydrogenase'''(PCD) catalyzes the reversible dehydrogenation of 1-pyrroline-5-carboxylate to glutamate using NAD or NADP as cofactors. PCD participates in glutamate, proline and arginine metabolism. PCD is the second enzyme in proline degradation hence it is important in stress conditions when plants accumulate proline<ref>PMID:15548746</ref>. See also [[Aldehyde dehydrogenase]].

== Disease ==

Mutation in PCD results in the metabolic disorder type II hyperprolinemia<ref>PMID:9700195</ref>.

== Structural highlights ==

PCD ligand <scene name='51/510199/Cv1/4'>glutarate binds in the cleft between the catalytic and NAD-binding domains</scene>. Water molecules are shown as red spheres. A <scene name='51/510199/Cv1/5'>cystein residue is the nucleophile attacker of the aldehyde</scene><ref>PMID:23928095</ref>.
</StructureSection>
==3D structures of pyrroline-5-carboxylate dehydrogenase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyrroline-5-carboxylate dehydrogenase

**[[3v9g]], [[4oe5]] – hPCD – human 
**[[3v9h]], [[3v9i]] – hPCD (mutant) 
**[[3v9j]], [[4lgz]], [[4e3x]] – mPCD – mouse 
**[[4oe6]] – yPCD – yeast 
**[[1uzb]] - TtPCD –''Termus thermophilus'' 
**[[4k57]] - TtPCD (mutant) 
**[[3qan]] – PCD – ''Bacillus halodurans'' 
**[[3rjl]] - PCD – ''Bacillus licheniformis'' 
**[[4idm]] – MtPCD – ''Mycobacterium tuberculosis'' 
**[[4ids]], [[4jdc]] - MtPCD (mutant) 

*PCD complex with cofactor

**[[3v9l]] - mPCD + NAD 
**[[7mer]], [[7mes]] – m1-PCD + NAD + hydroxyl-proline 
**[[4oe4]] - yPCD + NAD 
**[[2bhp]], [[2bja]] – TtPCD + NAD 
**[[2ehq]] - TtPCD + NADP 
**[[2bhq]] - TtPCD + glutamate + NAD 
**[[2bjk]] - TtPCD + citrate + NAD 
**[[2ehu]], [[2ejl]] - TtPCD + serine + NAD 
**[[2eii]] - TtPCD + valine + NAD 
**[[2eit]], [[2ejd]] - TtPCD + alanine + NAD 
**[[2eiw]], [[2ej6]], [[2j40]] - TtPCD + proline + NAD 
**[[2j5n]] - TtPCD + glycine + NAD 
**[[4ihi]] - MtPCD + NAD 
**[[4ns3]] - MtPCD (mutant) + cobalamin + NAD 

*PCD other complexes

**[[8rkr]], [[8rkq]] - hPCD + molecular tweezer 
**[[4lh0]] - mPCD + glyoxylate 
**[[4lh1]] - mPCD + malonate 
**[[4lh2]] - mPCD + succinate 
**[[4lh3]] - mPCD + glutarate 
**[[3v9k]] - mPCD + proline
**[[4lem]] - MtPCD (mutant) + cobalamin 
**[[2iy6]] - TtPCD + citrate 

}}
== References ==
<references/>
[[Category:Topic Page]]

Pyrroline-5-carboxylate dehydrogenase

2026-08-23T08:02:56Z

Michal Harel:

<StructureSection load='' size='350' side='right' caption='Mouse pyrroline-5-carboxylate dehydrogenase dimer complex with glutarate and PEG400 (PDB entry [[4lh3]])' scene='51/510199/Cv1/1'>
== Function ==
'''Pyrroline-5-carboxylate dehydrogenase''' or '''Delta-1-pyrroline-5-carboxylate dehydrogenase'''(PCD) catalyzes the reversible dehydrogenation of 1-pyrroline-5-carboxylate to glutamate using NAD or NADP as cofactors. PCD participates in glutamate, proline and arginine metabolism. PCD is the second enzyme in proline degradation hence it is important in stress conditions when plants accumulate proline<ref>PMID:15548746</ref>. See also [[Aldehyde dehydrogenase]].

== Disease ==

Mutation in PCD results in the metabolic disorder type II hyperprolinemia<ref>PMID:9700195</ref>.

== Structural highlights ==

PCD ligand <scene name='51/510199/Cv1/4'>glutarate binds in the cleft between the catalytic and NAD-binding domains</scene>. Water molecules are shown as red spheres. A <scene name='51/510199/Cv1/5'>cystein residue is the nucleophile attacker of the aldehyde</scene><ref>PMID:23928095</ref>.
</StructureSection>
==3D structures of pyrroline-5-carboxylate dehydrogenase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyrroline-5-carboxylate dehydrogenase

**[[3v9g]], [[4oe5]] – hPCD – human 
**[[3v9h]], [[3v9i]] – hPCD (mutant) 
**[[3v9j]], [[4lgz]], [[4e3x]] – mPCD – mouse 
**[[4oe6]] – yPCD – yeast 
**[[1uzb]] - TtPCD –''Termus thermophilus'' 
**[[4k57]] - TtPCD (mutant) 
**[[3qan]] – PCD – ''Bacillus halodurans'' 
**[[3rjl]] - PCD – ''Bacillus licheniformis'' 
**[[4idm]] – MtPCD – ''Mycobacterium tuberculosis'' 
**[[4ids]], [[4jdc]] - MtPCD (mutant) 

*PCD complex with cofactor

**[[3v9l]] - mPCD + NAD 
**[[7mer]], [[7mes]] – m1-PCD + NAD + hydroxyl-proline 
**[[4oe4]] - yPCD + NAD 
**[[2bhp]], [[2bja]] – TtPCD + NAD 
**[[2ehq]] - TtPCD + NADP 
**[[2bhq]] - TtPCD + glutamate + NAD 
**[[2bjk]] - TtPCD + citrate + NAD 
**[[2ehu]], [[2ejl]] - TtPCD + serine + NAD 
**[[2eii]] - TtPCD + valine + NAD 
**[[2eit]], [[2ejd]] - TtPCD + alanine + NAD 
**[[2eiw]], [[2ej6]], [[2j40]] - TtPCD + proline + NAD 
**[[2j5n]] - TtPCD + glycine + NAD 
**[[4ihi]] - MtPCD + NAD 
**[[4ns3]] - MtPCD (mutant) + cobalamin + NAD 

*PCD other complexes

**[[4lh0]] - mPCD + glyoxylate 
**[[4lh1]] - mPCD + malonate 
**[[4lh2]] - mPCD + succinate 
**[[4lh3]] - mPCD + glutarate 
**[[3v9k]] - mPCD + proline
**[[4lem]] - MtPCD (mutant) + cobalamin 
**[[2iy6]] - TtPCD + citrate 

}}
== References ==
<references/>
[[Category:Topic Page]]

Pyranose oxidase

2026-08-23T07:49:26Z

Michal Harel:

<StructureSection load='' size='350' side='right' caption='Pyranose oxidase complex with FAD and deoxy-fluoro-glucopyranose (PDB code [[3k4l]])' scene='70/708805/Cv/1'>
== Function ==
'''Pyranose oxidase''' or '''pyranose 2-oxidase''' (P2O) or '''C-glucosyl oxidoreductase''' catalyzes the conversion of D-glucose and molecular oxygen to 2-dehydro-D-glucose and H2O2. It is abundant in lignin-degrading white rot fungi. P2O is a <scene name='70/708805/Cv/7'>tetramer</scene> flavoprotein containing the <scene name='70/708805/Cv/8'>prosthetic group FAD in each monomer</scene>. P2O oxidizes several aldopyranoses with the preferred electron donors being D-glucose, D-xylose and D-sorbose<ref>PMID:11152063</ref>.

== Relevance ==

Converting common sugars and sugar derivatives with P2O provides a pool of sugar-derived intermediates for the synthesis of rare sugars, fine chemicals and drugs.

== Structural highlights ==
The <scene name='70/708805/Cv/9'>active site of P2O</scene> is gated by a highly conserved loop which determines the substrate specificity. Water molecules are shown as red spheres. The active site contains the FAD cofactor<ref>PMID:20528921</ref>.
</StructureSection>

== 3D Structures of pyranose oxidase ==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyranose oxidase

**[[1tzl]] – PeP2O + FAD – ''Peniophora'' 
**[[2f6c]] – PeP2O (mutant) + FAD 
**[[3bg6]], [[3bg7]], [[3bly]], [[3fdy]] – TmP2O (mutant) + FAD – ''Trametes multicolor'' 
**[[1tt0]], [[2igk]] – ToP2O + FAD – ''Trametes ochracea'' 
**[[2igm]], [[2ign]], [[3k4b]], [[3k4c]], [[3k4j]], [[3k4k]], [[3k4n]], [[3lsh]], [[3lsi]], [[3lsk]], [[4mok]] – ToP2O (mutant) + FAD 
**[[4mif]], [[4mig]] – ToP2O + FAD derivative 
**[[3lsm]] – ToP2O (mutant) + FAD derivative 
**[[9fl2]] – P2O + FAD – ''Oscillatoria principes'' 
**[[8qve]] – P2O + FAD – ''Deinococcus aerius'' 

*Pyranose oxidase complex

**[[2f5v]] – PeP2O (mutant) + FAD + keto-glucose 
**[[2igo]], [[3k4l]], [[3k4m]], [[4mih]] – ToP2O (mutant) + FAD + deoxy-fluoro-glucopyranose 
**[[4moe]], [[4mof]], [[4mog]], [[4moh]], [[4moi]], [[4moj]], [[4mol]] – ToP2O (mutant) + FAD derivative + deoxy-fluoro-glucopyranose 
**[[4mom]], [[4mop]], [[4moq]], [[4mor]] – ToP2O (mutant) + FAD derivative + deoxy-fluoro-galactopyranose 
**[[4moo]] – ToP2O (mutant) + FAD derivative + deoxy-fluoro-galactose 
**[[4mos]] – ToP2O (mutant) + FAD derivative + deoxy-fluoro-galactopyranose + deoxy-fluoro-galactose 
**[[3pl8]] – ToP2O (mutant) + FAD + deoxy-fluoro-glucose 

}}
== References ==
<references/>
[[Category:Topic Page]]

Pyranose oxidase

2026-08-23T07:29:56Z

Michal Harel:

<StructureSection load='' size='350' side='right' caption='Pyranose oxidase complex with FAD and deoxy-fluoro-glucopyranose (PDB code [[3k4l]])' scene='70/708805/Cv/1'>
== Function ==
'''Pyranose oxidase''' or '''pyranose 2-oxidase''' (P2O) or '''C-glucosyl oxidoreductase''' catalyzes the conversion of D-glucose and molecular oxygen to 2-dehydro-D-glucose and H2O2. It is abundant in lignin-degrading white rot fungi. P2O is a <scene name='70/708805/Cv/7'>tetramer</scene> flavoprotein containing the <scene name='70/708805/Cv/8'>prosthetic group FAD in each monomer</scene>. P2O oxidizes several aldopyranoses with the preferred electron donors being D-glucose, D-xylose and D-sorbose<ref>PMID:11152063</ref>.

== Relevance ==

Converting common sugars and sugar derivatives with P2O provides a pool of sugar-derived intermediates for the synthesis of rare sugars, fine chemicals and drugs.

== Structural highlights ==
The <scene name='70/708805/Cv/9'>active site of P2O</scene> is gated by a highly conserved loop which determines the substrate specificity. Water molecules are shown as red spheres. The active site contains the FAD cofactor<ref>PMID:20528921</ref>.
</StructureSection>

== 3D Structures of pyranose oxidase ==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Pyranose oxidase

**[[1tzl]] – PeP2O + FAD – ''Peniophora'' 
**[[2f6c]] – PeP2O (mutant) + FAD 
**[[3bg6]], [[3bg7]], [[3bly]], [[3fdy]] – TmP2O (mutant) + FAD – ''Trametes multicolor'' 
**[[1tt0]], [[2igk]] – ToP2O + FAD – ''Trametes ochracea'' 
**[[2igm]], [[2ign]], [[3k4b]], [[3k4c]], [[3k4j]], [[3k4k]], [[3k4n]], [[3lsh]], [[3lsi]], [[3lsk]], [[4mok]] – ToP2O (mutant) + FAD 
**[[4mif]], [[4mig]] – ToP2O + FAD derivative 
**[[3lsm]] – ToP2O (mutant) + FAD derivative 

*Pyranose oxidase complex

**[[2f5v]] – PeP2O (mutant) + FAD + keto-glucose 
**[[2igo]], [[3k4l]], [[3k4m]], [[4mih]] – ToP2O (mutant) + FAD + deoxy-fluoro-glucopyranose 
**[[4moe]], [[4mof]], [[4mog]], [[4moh]], [[4moi]], [[4moj]], [[4mol]] – ToP2O (mutant) + FAD derivative + deoxy-fluoro-glucopyranose 
**[[4mom]], [[4mop]], [[4moq]], [[4mor]] – ToP2O (mutant) + FAD derivative + deoxy-fluoro-galactopyranose 
**[[4moo]] – ToP2O (mutant) + FAD derivative + deoxy-fluoro-galactose 
**[[4mos]] – ToP2O (mutant) + FAD derivative + deoxy-fluoro-galactopyranose + deoxy-fluoro-galactose 
**[[3pl8]] – ToP2O (mutant) + FAD + deoxy-fluoro-glucose 

}}
== References ==
<references/>
[[Category:Topic Page]]

Pteridine reductase

2026-08-23T07:16:39Z

Michal Harel:

<StructureSection load='' size='350' side='right' caption='Structure of pteridine reductase complex with NADPH, tetrahydrobiopterin, ethanediol and ethylene glycol (PDB entry [[2bfp]])' scene='54/547078/Cv/1'>

== Function ==
'''Pteridine reductase''' (PTR) catalyzes the reduction of 5,6,7,8-tetrahydrobiopterin (THBP) to biopterin. PTR is part of pterin and folate metabolism<ref>PMID:12651944</ref>. NADP is the hydrogen acceptor in this reduction.

== Relevance ==
PTR is essential for growth of trypanosomatid protozoans like Leishmania parasites, thus PTR inhibitors like methotrexate (MTX) or triaminoquinazoline (TAQ) are tested as potential drugs<ref>PMID:18245389</ref>.

== Structural highlights ==
<scene name='54/547078/Cv/3'>Six residues (colored in deepskyblue) are important for creating the active site, substrate binding or implicated in catalysis</scene><ref>PMID:16055151</ref>. Water molecules are shown as red spheres.
</StructureSection>

==3D structures of pteridine reductase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Pteridine reductase'''

**[[2xox]] – LdPTR1 (mutant) – ''Leishmania donovani'' 
**[[2bfo]] – LmPTR1 + NADPH – ''Leishmania major'' 

*Pteridine reductase complex with inhibitor

**[[1e7w]] – LmPTR1 + NADPH + MTX 
**[[1w0c]] – LmPTR1 + NADPH + TAQ 
**[[2bfa]], [[2bfm]], [[3h4v]], [[5l42]], [[5l4n]], [[6rxc]] – LmPTR1 + NADPH + inhibitor 
**[[1p33]] – PTR1 + NADPH + MTX – ''Leishmania tarentolae'' 
**[[1mxf]] – TcPTR2 + NADPH + MTX – ''Trypanosoma cruzi'' 
**[[2c7v]] – TbPTR1 + NADPH + MTX – ''Trypanosoma brucei'' 
**[[2vz0]], [[2wd7]], [[2wd8]], [[2x9g]], [[2x9n]], [[2x9v]], [[2yhi]], [[2yhu]], [[3bmn]], [[3bmo]], [[3bmq]], [[3gn1]], [[3gn2]], [[3jq6]], [[3jq7]], [[3jq8]], [[3jq9]], [[3jqa]], [[3jqb]], [[3jqc]], [[3jqd]], [[3jqe]], [[3jqf]], [[3jqg]], [[3mcv]], [[4cl8]], [[4cld]], [[4cle]], [[4clh]], [[4clo]], [[4clr]], [[4clx]], [[4cm1]], [[4cm3]], [[4cm4]], [[4cm5]], [[4cm6]], [[4cm7]], [[4cm8]], [[4cm9]], [[4cma]], [[4cmb]], [[4cmc]], [[4cme]], [[4cmg]], [[4cmi]], [[4cmj]], [[4cmk]], [[4wcd]], [[4wcf]], [[5izc]], [[5jcj]], [[5jcx]], [[5jdc]], [[5jdi]], [[5k6a]], [[6gck]], [[6gcl]], [[6gcp]], [[6gcq]], [[6gd0]], [[6gd4]], [[6gdo]], [[6gdp]], [[6gex]], [[6gey]], [[6rx0]], [[6rx5]], [[6rx6]], [[6tbx]], [[7opj]], [[8of2]], [[8r3i]], [[8rhu]], [[8rhv]], [[8rhx]], [[8rhy]], [[9hup]], [[9hut]], [[9huu]], [[9huv]], [[9huw]], [[9qdk]] – TbPTR1 + NADPH + inhibitor 
**[[6hnc]], [[6hnr]], [[6how]] – TbPTR1 + NADPH + cycloguanyl derivative 

*Pteridine reductase complex with ligand

**[[2bfp]] – LmPTR1 + NADPH + THBP 
**[[2qhx]] – LmPTR1 + NADPH + ligand 
**[[1e92]], [[2bf7]] – LmPTR1 + NADPH + DHBP 
**[[7pxx]] – LmPTR1 + NADPH + folate 
**[[1mxh]] – TcPTR1 + NADPH + folate 
**[[3bmc]] – TbPTR1 + NADPH + folate 
}}
== References ==
<references/>
[[Category:Topic Page]]

Pyrin domain 3D structures

2026-08-20T09:18:50Z

Michal Harel:

== 3D Structures of Pyrin domain ==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}

[[4im6]] – hPYD in NLRP1 – human 
[[6x6a]], [[6x6c]] - hPYD in NLRP1 + DPP9 
[[4ifp]] - hPYD in NLRP1/MBP 
[[2naq]] - hPYD in NLRP3 - NMR 
[[6npy]] - hPYD in NLRP3 + NEK7 - Cryo EM 
[[4ewi]] - hPYD in NLRP4 
[[6ncv]] - hPYD in NLRP6 - Cryo EM 
[[6ndj]] - hPYD in NLRP6/MBP 
[[2km6]] – hPYD in NLRP7 – NMR 
[[6z2g]] - hPYD in NLRP9 
[[2m5v], [[7bso]]] - hPYD in NLRP10 
[[2l6a]] - hPYD in NLRP12 - NMR 
[[4xhs]] - hPYD in NLRP12/MBP 
[[4n1j]], [[4n1k]], [[4n1l]] - hPYD in NLRP14 
[[4o7q]] - hPYD (mutant) in AIM2 
[[3vd8]] - hPYD in AIM2/MBP 
[[2wl1]] – hPYD PRYSPRY residues 586-776 
[[1pn5]] – hPYD in NALP1 - NMR 
[[3qf2]] - hPYD in NALP3 
[[1ucp]] - hPYD in apoptosis-associated speck-like protein – NMR 
[[2hm2]] – hPYD in apoptosis-associated speck-like protein2 – NMR 
[[2dbg]] – hPYD in myeloid cell nuclear differentiation antigen - NMR 
[[2mpc]] - hPYD in pyrin - NMR 
[[2do9]] – mPYD in NALP10 – mouse – NMR 
[[2yu0]] – mPYD in interferon-activable protein 205 - NMR 
[[7lfh]] - mPYD in NLRP3 - Cryo EM 
[[9sfp]], [[9t63]], [[9t66]], [[9t67]], [[9t68]], [[9w2m]], [[9xrl]], [[12dl]], [[24mc]] - mPYD in CPL - Cryo EM 

[[Category:Topic Page]]

Pyrin domain

2026-08-20T08:57:27Z

Michal Harel:

Pyrin domain 3D structures

2026-08-20T08:56:37Z

Michal Harel: Created page with "== 3D Structures of Pyrin domain == Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} 4im6 – hPYD in NLRP1 – human 6x6a, 6x6c - hPYD in NLRP1 + DPP9 4ifp - hPYD in NLRP1/MBP 2naq - hPYD in NLRP3 - NMR 6npy - hPYD in NLRP3 + NEK7 - Cryo EM 4ewi - hPYD in NLRP4 6ncv - hPYD in NLRP6 - Cryo EM 6ndj - hPYD in NLRP6/MBP 2km6 – hPYD in NLRP7 – NMR [..."

Pyrin domain

2026-08-20T08:54:49Z

Michal Harel:

<StructureSection load='' size='450' side='right' caption='NMR structure of pyrin domain in human NLRP7, [[2km6]]' scene='Pyrin_domain/Pyrin_domain/1 ' pspeed='8'>

== Function ==
'''Pyrin domain''' (PYD) is a protein domain known as death fold. This domain allows the protein to interact with other pyrin domains. It is also known as PYD or PAAD/DAPIN or marenostrin domain. Proteins containing pyrin domain are involved in inflammation and apoptosis. The NALP proteins contain domains NACHT, LRR and PYD and are part of the inflammasome. A 781-amino acid protein named pyrin contains a PYD domain in its N-terminal<ref>PMID:11514682</ref>.

== Disease ==
Mutations in the protein are the cause of Familial Mediterranean fever<ref>PMID:17431422</ref>.

</StructureSection>
== 3D Structures of Pyrin domain ==

[[Pyrin domain 3D structures]]

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}

[[4im6]] – hPYD in NLRP1 – human 
[[6x6a]], [[6x6c]] - hPYD in NLRP1 + DPP9 
[[4ifp]] - hPYD in NLRP1/MBP 
[[2naq]] - hPYD in NLRP3 - NMR 
[[6npy]] - hPYD in NLRP3 + NEK7 - Cryo EM 
[[4ewi]] - hPYD in NLRP4 
[[6ncv]] - hPYD in NLRP6 - Cryo EM 
[[6ndj]] - hPYD in NLRP6/MBP 
[[2km6]] – hPYD in NLRP7 – NMR 
[[6z2g]] - hPYD in NLRP9 
[[2m5v], [[7bso]]] - hPYD in NLRP10 
[[2l6a]] - hPYD in NLRP12 - NMR 
[[4xhs]] - hPYD in NLRP12/MBP 
[[4n1j]], [[4n1k]], [[4n1l]] - hPYD in NLRP14 
[[4o7q]] - hPYD (mutant) in AIM2 
[[3vd8]] - hPYD in AIM2/MBP 
[[2wl1]] – hPYD PRYSPRY residues 586-776 
[[1pn5]] – hPYD in NALP1 - NMR 
[[3qf2]] - hPYD in NALP3 
[[1ucp]] - hPYD in apoptosis-associated speck-like protein – NMR 
[[2hm2]] – hPYD in apoptosis-associated speck-like protein2 – NMR 
[[2dbg]] – hPYD in myeloid cell nuclear differentiation antigen - NMR 
[[2mpc]] - hPYD in pyrin - NMR 
[[2do9]] – mPYD in NALP10 – mouse – NMR 
[[2yu0]] – mPYD in interferon-activable protein 205 - NMR 
[[7lfh]] - mPYD in NLRP3 - Cryo EM 

== References ==
<references/>

[[Category:Topic Page]]

Pyridoxine 5'-phosphate oxidase

2026-08-20T08:43:48Z

Michal Harel:

<StructureSection load='' size='350' side='right' scene='48/486466/Cv/1' caption='Pyridoxine 5-phosphate oxidase dimer complex with pyridoxine 5-phosphate, [[2aq6]]' >
== Function ==
'''Pyridoxine 5’-phosphate oxidase''' or '''Pyridoxamine 5’-phosphate oxidase''' (PNPO) catalyzes the oxidation of pyridoxamine-phosphate by molecular oxygen producing pyridoxal 5’-phosphate, ammonia and hydrogen peroxide. Pyridoxal 5’-phosphate (PLP), commonly known as vitamin B6, is a biological essential cofactor. PNPO catalyzes the last step in vitamin B6 metabolism. PNPO uses FMN as cofactor<ref>PMID:12686112</ref>.

== Disease ==
PNPO mutations are present in epilepsy patients<ref>PMID:24645144</ref>.

== Structural highlights ==

The active site of PNPO shows the product of PNPO catalysis - <scene name='48/486466/Cv/4'>PLP - interacting with both subunits of the enzyme</scene><ref>PMID:16239726</ref>. Water molecules are shown as red spheres.
</StructureSection>
==3D structures of pyridoxine 5'-phosphate oxidase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}

[[1nrg]], [[8qyt]] - hPNPO + PLP – human 
[[8ros]] - hPNPO + PLP derivative 
[[3hy8]] - hPNPO (mutant) + PLP 
[[6h00]], [[8qyw]] – hPNPO (mutant) + FMN 
[[2aq6]] - MtPNPO + PLP – ''Mycobacterium tuberculosis'' 
[[1y30]] - MtPNPO + FMN 
[[1xxo]] - MtPNPO 
[[1dnl]], [[1g76]], [[1wv4]] – EcPNPO – ''Escherichia coli'' 
[[1g76]], [[1g77]], [[1g78]], [[1g79]], [[1jnw]] – EcPPO + PLP 
[[6ylz]] – EcPNPO (mutant) + FMN + Pi 
[[6ymh]] – EcPNPO (mutant) + FMN + PLP 
[[4hmw]] – BlPNPO + FMN – ''Burkholderia lata'' 
[[4hmx]] – BlPNPO + FMN + phenazine carboxylic acid 
[[4hms]] – PfPNPO + FMN – ''Pseudomonas fluorescense'' 
[[4hmt]], [[4hmu]], [[4hmv]] – PfPNPO + FMN + phenazine carboxylic acid 

== References ==
<references/>
[[Category:Topic Page]]

Pyridoxal kinase

2026-08-20T07:54:50Z

Michal Harel:

<StructureSection load='' size='400' side='right' scene='54/543357/Cv/1' caption='E. Coli pyridoxal kinase 1 complex with pyridoxal [[2ddw]]'>
== Function ==
'''Pyridoxal kinase''' (PDX) catalyzes the transfer of phosphate (Pi) from ATP to 5’ alcohol of pyridoxine, pyridoxamine and pyridoxal<ref>PMID:25655354</ref>.

== Structural highlights ==

<scene name='54/543357/Cv/4'>PDX1 active site</scene><ref>PMID:16740960</ref>.
</StructureSection>
== 3D Structures of pyridoxal kinase ==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Pyridoxal kinase'''

**[[2f7k]] – hPDX - human 
**[[1lhp]] – sPDX – sheep 
**[[6yjz]] – mPDX - mouse 
**[[2ddm]] – EcPDX1 – ''Escherichia coli'' 
**[[3h74]] – LpPDX – ''Lactobacillus planarum'' 
**[[3zs7]] – PDX – ''Trypanosoma brucei'' 
**[[4c5j]] – SaPDX – ''Staphylococcus aureus'' 
**[[5tqi]] - PDX - ''Burkholderia multivorans'' 
**[[5trw]] - PDX - ''Burkholderia xenovorans'' 
**[[5b6a]] - PDX - ''Pseudomonas aeruginosa'' 
**[[5zw9]] – ScPDX – ''Salmonella choleraesuis'' 

*Pyridoxal kinase complex with pyridoxal compounds

**[[3fhx]] – hPDX (mutant) + Mg + Na + ATP + pyridoxal + PLP 
**[[3keu]] – hPDX + Mg + ATP + PLP 
**[[1rft]] – sPDX + Zn + K + AMPPCP + pyridoxamine 
**[[1rfu]] – sPDX + Zn + ADP + PLP 
**[[2ddw]] – EcPDX1 + pyridoxal 
**[[4c5l]] – SaPDX + pyridoxal 
**[[4c5n]] – SaPDX + pyridoxal + AMPPCP 
**[[4s1i]] – EhPDX + Mg + PLP - ''Entamoeba histolytica'' 
**[[6su9]] – PDX + pyridoxal + AMPPNP – ''Plasmodium falciparum'' 
**[[6k91]], [[6k92]] – LdPDX + ADP + pyridoxine derivative – ''Leishmania donovani'' 
**[[6k90]] – LdPDX + ADP + pyridoxamine 
**[[5zwa]], [[5zwb]] – ScPDX + ADP + PLP 

*Other pyridoxal kinase complexes

**[[2ajp]] – hPDX + Mg + ANP 
**[[2yxt]] – hPDX + Na + Pi 
**[[2yxu]] – hPDX + Mg + Na + ATP + Pi 
**[[3fhy]] – hPDX (mutant) + Mg + Na + ATP 
**[[4en4]] – hPDX + Mg + ATP + ginkotoxin 
**[[4eoh]] – hPDX + Na + theophylline 
**[[8wr2]] – hPDX + Na + luteoline 
**[[1lhr]] – sPDX + Zn + K + ATP 
**[[1rfv]] – sPDX + Zn + ADP 
**[[1ygj]], [[1ygk]], [[1yhj]] – sPDX + roscovitine 
**[[6yk0]] – mPDX + ATPgS 
**[[6yk1]] – mPDX + ATPgS + artesunate 
**[[2ddo]] – EcPDX1 + Mg + ATP + Pi 
**[[2i5b]] – PDX + ADP – ''Bacillus subtilis'' 
**[[6k8z]] – LdPDX + ADP 
**[[3hyo]] – LpPDX + Mg + ADP 
**[[3ibq]] – LpPDX + Mg + ATP 
**[[4c5k]] – SaPDX + ADP 
**[[4c5m]] – SaPDX + AMPPCP 
**[[4s1m]] – EhPDX + Mg 
**[[4s1h]] – EhPDX + Mg + ADP 

}}
== References ==
<references/>
[[Category:Topic Page]]

Purine repressor

2026-08-20T07:41:52Z

Michal Harel:

<StructureSection load='' size='450' side='right' caption='Structure of E. coli purine processor complex with DNA and guanine (PDB entry [[1wet]])' scene='55/554904/Cv/1'>
== Function ==
'''Purine repressor''' (PurR) is a member of the lac repressor family. PurP binds DNA via a highly conserved helix-turn-helix at the N terminal (DBD). PurP contains a nucleotide co-repressor binding domain as well (CBD). PurP binds to a 16-bp operator sequence and co-regulates genes which are involved in the biosynthesis of purine and pyrimidine nucleotides<ref>PMID:1971621</ref>.

== Structural highlights ==
The <scene name='55/554904/Cv/5'>PurP guanine co-repressor binding site includes stacking interactions as well as hydrogen bonded ones</scene>. Water molecules are shown as red spheres. The DNA binding domain contains a <scene name='55/554904/Cv/6'>helix-turn-helix-loop-helix motif which interacts with the DNA major groove</scene> and a hinge helix binding to to the DNA minor groove. <scene name='55/554904/Cv/7'>Residue L54 interdigitates with the DNA central base pair</scene><ref>PMID:9278422</ref>.
</StructureSection>

==3D structures of purine repressor==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Purine repressor

**[[1pru]], [[1prv]] - EcPurR DBD – ''Escherichia coli'' - NMR 
**[[1dbq]] - EcPurR CBD + Mg - NMR 
**[[1jhz]] - EcPurR CBD (mutant) + Mg 
**[[1o57]] - BsPurR - ''Bacillus subtilis'' 

*Purine repressor complex with DNA and nucleotide

**[[1bdi]], [[1pnr]], [[1qp0]], [[1qp4]], [[1qpz]], [[1qqb]] - EcPurR + DNA + hypoxanthine 
**[[1bdh]], [[1jfs]], [[1jft]], [[1jh9]], [[1qp7]], [[1qqa]], [[1vpw]], [[2pud]], [[2pug]] - EcPurR (mutant) + DNA + hypoxanthine 
**[[1wet]] - EcPurR + DNA + guanine 
**[[2pua]] - EcPurR (mutant) + DNA + methylpurine 
**[[2pub]], [[2pue]] - EcPurR (mutant) + DNA + adenine 
**[[2puc]], [[2puf]] - EcPurR (mutant) + DNA + guanine 
**[[1zay]] - EcPurR + DNA + hypoxanthine + di-imino-purine 
**[[7rmw]] – BsPurR + PPGPP 
}}
== References ==
<references/>
[[Category:Topic Page]]

Pseudouridine synthase 3D structures

2026-08-20T07:19:55Z

Michal Harel:

== 3D Structures of pseudouridine synthase ==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

* Pseudouridine synthase or tRNA pseudouridine synthase

**[[4iqm]], [[4its]], [[4j37]], [[4nz6]] – hPUS1 catalytic domain 83-394 - human 
**[[4nz7]] - hPUS1 catalytic domain (mutant) 
**[[9f9q]] – hPUS3 (mutant) – Cryo EM 
**[[5vbb]] – hPUS C-like 
**[[8jfx]] – hPUS TruB 58-318 
**[[7mzv]] – yPUS7 - yeast 
**[[1ze1]] – TmPUS B – Thermotoga maritima >
**[[1vio]] - HiPUS RsuA – Haemophilus influenzae 
**[[6gut]] – HiPUS/PILA 
**[[1dj0]] – EcPUS I – Escherichia coli 
**[[1ksk]], [[1ksl]], [[1ksv]] – EcPUS RsuA 
**[[4lab]] - EcPUS RluB catalytic domain 
**[[1xpi]] - EcPUS RluC catalytic domain 
**[[1v9k]] - EcPUS RluC C-terminal domain (mutant) 
**[[2ist]] - EcPUS RluD 
**[[1prz]], [[1qyu]], [[1v9f]] - EcPUS RluD catalytic domain 
**[[2olw]] - EcPUS RluE 
**[[2oml]] - EcPUS RluE catalytic domain 
**[[2gml]] - EcPUS RluF catalytic domain 
**[[1si7]], [[1szw]], [[1sb7]] - EcPUS TruD 
**[[1vs3]] – PUS TruA – Thermus thermophilus 
**[[1sgv]] – PUS TruB – Mycobacterium tuberculosis 
**[[8q70]] – PfPUS A – Pyrococcus furiosus 

* Pseudouridine synthase complex with RNA

**[[8okd]], [[9enb]], [[9enc]], [[9ene]], [[9enf]] – hPUS3 + tRNA – Cryo EM 
**[[9h51]] – hPUS1 in 28S ribosome – Cryo EM 
**[[7r9f]] – yPUS1 + RNA 
**[[7r9g]] – yPUS1 (mutant) + RNA 
**[[1k8w]] – EcPUS B + stem-loop RNA 
**[[9cl9]] – EcPUS B in 50S ribosome – Cryo EM 
**[[7bl5]] – EcPUS D in 50S ribosome – Cryo EM 
**[[1zl3]] - EcPUS B (mutant) + stem-loop RNA 
**[[2i82]] – EcPUS RluA + RNA 
**[[4lgt]] – EcPUS RluB + RNA 
**[[3dh3]] - EcPUS RluF + RNA 
**[[2nqp]], [[2nr0]], [[2nre]] – EcPUS TruA + Leu-tRNA 
**[[1r3e]], [[1r3f]] - EcPUS B + RNA 
**[[3hjw]], [[3lwo]], [[3lwp]], [[3lwq]], [[3lwr]], [[3lwv]] – PfPUS Cbf5 + ribosome biogenesis protein Nop10 + ribosomal protein L7 + RNA 
**[[3mqk]] - PfPUS Cbf5 + ribosome biogenesis protein Nop10 + small nuclear RNP Gar1-like protein + RNA 
**[[3hjy]] - PfPUS Cbf5 + ribosome biogenesis protein NOP10 + RNA 
**[[1ze2]] - TmPUS B + RNA 
**[[2ab4]] - TmPUS B (mutant) + RNA 
**[[6yxx]], [[6yxy]], [[7aoi]] – TbPUS in 50S ribosome – Trypanosoma brucei - Cryo EM 
**[[9hny]] – TbPUS in 30S ribosome - Cryo EM 
**[[7am2]] – PUS in 50S ribosome – Leishmania tarntolae - Cryo EM 

* Probable pseudouridine synthase

**[[2apo]] – PPUS + ribosome biogenesis protein Nop10 – ''Methanocaldococcus jannaschii'' 
**[[2ey4]] - PfPPUS Cbf5 + ribosome biogenesis protein Nop10 + small nucleolar RNP 
**[[2hvy]], [[3hax]] - PfPPUS B + ribosome biogenesis protein Nop10 + ribosomal protein L7 + RNA 
**[[2rfk]] - PfPUS B + ribosome biogenesis protein Nop10 + small nucleolar RNP + RNA 
**[[3hay]] - PfPPUS B + ribosome biogenesis protein Nop10 + ribosomal protein L7 + small nucleolar RNP + RNA 
**[[2aus]] – PPUS B + ribosome biogenesis protein Nop10 – ''Pyrococcus abyssi'' 
**[[1z2z]] – PPUS D – ''Methanosarcina mazei'' 
}}

[[Category:Topic Page]]

Pseudopilin

2026-08-19T10:11:24Z

Michal Harel:

<StructureSection load='3ci0' size='350' side='right' scene='' caption='E. coli minor pseudopilins: GspI (wheat), GspJ (blue), GspK (dark red) complex with Cl- (deep green) and Ca+2 ion (light green) (PDB code [[3ci0]])'>

'''Pseudopilin''' is a protein component of the type 2 secretion system complex. The complex is thought to be composed in ''E. coli'' of a '''major pseudopilin''' or '''general secretion pathway protein G''' ('''GspG or EspG or PulG''') and several '''minor pseudopilins''' or '''general secretion pathway proteins H, I, J, K''' ('''GspI, GspJ, GspK or EspI, EspJ, EspK, EspH, PulH, PulI, PulJ, PulK''')<ref>PMID:22157749</ref>.

</StructureSection>
==3D structures of pseudopilin==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*Minor pseudopilin or EpsH, EpsI, EpsJ, EpsK, PulH, PulI, PulJ, PulK, FimU, XcpW, XcpV, XcpX

**[[2ret]] – VvEpsI (mutant) + EpsJ – ''Vibrio vulnificus''

**[[3cfi]] - VvEpsI + EpsJ 
**[[2qv8]] - VvEpsH 
**[[4dq9]] - EpsH - ''Vibrio cholerae'' 
**[[3nje]] - PaEpsJ - ''Pseudomonas aeruginosa'' 
**[[3nje]] - PaXcpW 
**[[6utu]] – PaXcpW + PaXcpV + PaXcpX 
**[[9a1e]] – PaXcpH + PaXcpI + PaXcpJ + XcpK - integrative 
**[[4ipu]], [[4ipv]] - PaFimU 
**[[5bw0]] - PaEpsJ + EpsI 
**[[5vtm]] - PaEpsJ + EpsK + EpsI 
**[[3ci0]] – EcGspI + GspJ + GspK – ''Escherichia coli'' 
**[[2knq]] - EcGspH - NMR 

*Major pseudopilin or EpsG or PulG

**[[3gn9]], [[4lw9]], [[3fu1]] - VvEpsG 
**[[3g20]] - EcGspG 
**[[1t92]] - PulG - ''Klebsiella pneumoniae'' 
**[[5wda]] - KoPulG - ''Klebsiella oxytoca'' 
**[[5o2y]] - KoPulG - NMR 
**[[2kep]] - PaPulG - NMR 
}}

== References ==
<references/>

[[Category:Topic Page]]

Pseudoazurin

2026-08-19T10:00:11Z

Michal Harel:

<StructureSection load='' size='340' side='right' caption='Structure of pseudoazurin complex with Cu+2 ion (orange) (PDB code [[1pza]]).' scene='59/593961/Cv/1'>

== Function ==

'''Pseudoazurin''' (PAZ) transfers electrons to and from nitrite reductase. PAZ is found in denitrifying bacteria. PAZ contains a single copper atom<ref>PMID:20945335</ref>.

== Structural highlights ==

The <scene name='59/593961/Cv/4'>PAZ copper is bound in a approximately tetrahedral geometry</scene>.<ref>PMID:8034003</ref>.
</StructureSection>

==3D structures of pseudoazurin==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}

[[1pzc]] – AfPAZ – ''Alcaligenes faecalis'' 
[[1paz]], [[1pza]], [[1pzb]], [[3paz]], [[5x31]], [[8k9n]], [[8k9p]] – AfPAZ + Cu+2 
[[3nyk]] – AfPAZ + Co+2 
[[4paz]], [[5paz]], [[6paz]], [[7paz]], [[8paz]] – AfPAZ (mutant) + Cu+2 
[[4rh4]] - AfPAZ + Zn+2 
[[4rh4]] – AfPAZ (mutant) + Zn+2 
[[1py0]] – AfPAZ (mutant) + Zn+2 + Y+2 
[[2p80]] – AfPAZ + Cu+2 + Cu-containing nitrite reductase - NMR 
[[1bqk]], [[1bqr]], [[1zia]], [[1zib]], [[2ux6]], [[2ux7]], [[2uxf]], [[2uxg]] – AcPAZ + Cu+2 – ''Achromobacter cycloclastes'' 
[[2jkw]], [[8wqz]], [[5xmo]], [[5y23]], [[5ysg]], [[5yw3]], [[5z0x]], [[5ztd]], [[6akn]], [[6ifp]], [[8hm9]], [[8wqz]], [[9m62]], [[9w3y]] – AcPAZ (mutant) + Cu+2 
[[3ef4]] – PAZ + Cu+2 – ''Hyphomicrobium denitrificans'' 
[[1adw]], [[3erx]], [[4bwt]] – PpPAZ + Cu+2 – ''Paracoccus pantotrophus'' 
[[4bwu]], [[4bxv]] – PpPAZ (mutant) + Cu+2 
[[1pmy]] – PAZ + Cu+2 – ''Methylobacterium extorquens'' 
[[3tu6]] – PAZ + Cu+2 – ''Sinorhizobium meliloti'' 
[[5b1j]] - PAZ + copper-containing nitrite reductase + Cu+2 - ''Hyphomicrobium denitrificans'' 

== References ==
<references/>

[[Category:Topic Page]]

Pseudoazurin

2026-08-19T09:59:15Z

Michal Harel:

<StructureSection load='' size='340' side='right' caption='Structure of pseudoazurin complex with Cu+2 ion (orange) (PDB code [[1pza]]).' scene='59/593961/Cv/1'>

== Function ==

'''Pseudoazurin''' (PAZ) transfers electrons to and from nitrite reductase. PAZ is found in denitrifying bacteria. PAZ contains a single copper atom<ref>PMID:20945335</ref>.

== Structural highlights ==

The <scene name='59/593961/Cv/4'>PAZ copper is bound in a approximately tetrahedral geometry</scene>.<ref>PMID:8034003</ref>.
</StructureSection>

==3D structures of pseudoazurin==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}

[[1pzc]] – AfPAZ – ''Alcaligenes faecalis'' 
[[1paz]], [[1pza]], [[1pzb]], [[3paz]], [[5x31]], [[8k9n]], [[8k9p]] – AfPAZ + Cu+2 
[[3nyk]] – AfPAZ + Co+2 
[[4paz]], [[5paz]], [[6paz]], [[7paz]], [[8paz]] – AfPAZ (mutant) + Cu+2 
[[4rh4]] - AfPAZ + Zn+2 
[[4rh4]] – AfPAZ (mutant) + Zn+2 
[[1py0]] – AfPAZ (mutant) + Zn+2 + Y+2 
[[2p80]] – AfPAZ + Cu+2 + Cu-containing nitrite reductase - NMR 
[[1bqk]], [[1bqr]], [[1zia]], [[1zib]], [[2ux6]], [[2ux7]], [[2uxf]], [[2uxg]] – AcPAZ + Cu+2 – ''Achromobacter cycloclastes'' 
[[2jkw]], [[8wqz]], [[5xmo]], [[5y23]], [[5ysg]], [[5yw3]], [[5z0x]], [[5ztd]], [[6akn]], [[6ifp]] – AcPAZ (mutant) + Cu+2 
[[3ef4]] – PAZ + Cu+2 – ''Hyphomicrobium denitrificans'' 
[[1adw]], [[3erx]], [[4bwt]] – PpPAZ + Cu+2 – ''Paracoccus pantotrophus'' 
[[4bwu]], [[4bxv]] – PpPAZ (mutant) + Cu+2 
[[1pmy]] – PAZ + Cu+2 – ''Methylobacterium extorquens'' 
[[3tu6]] – PAZ + Cu+2 – ''Sinorhizobium meliloti'' 
[[5b1j]] - PAZ + copper-containing nitrite reductase + Cu+2 - ''Hyphomicrobium denitrificans'' 

== References ==
<references/>

[[Category:Topic Page]]

Serine/threonine protein kinase 3D structures

2026-08-19T08:13:40Z

Michal Harel:

==3D structures of serine/threonine protein kinase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Chk1'''; domains - kinase 1-289; KA1 393-492
**[[1ia8]] – hChk1 kinase domain – human
**[[5w12]] – hChk1 KA1 domain
**[[1zlt]] – hChk1 kinase domain + hymenaldisine
**[[1nvq]], [[1nvr]] – hChk1 kinase domain + peptide + saurosporine
**[[1nvs]], [[1zys]], [[7ako]] - hChk1 kinase domain + peptide + inhibitor
**[[7akm]] - hChk1 kinase domain + ATP
**[[2ayp]], [[2br1]], [[2brb]], [[2brg]], [[2brh]], [[2brm]], [[2brn]], [[2bro]], [[2c3j]], [[2c3k]], [[2c3l]], [[2cgu]], [[2cgv]], [[2cgw]], [[2cgx]], [[2e9n]], [[2e9o]], [[2e9p]], [[2e9u]], [[2e9v]], [[2gdo]], [[2ghg]], [[2hog]], [[2hxl]], [[2hxq]], [[2hy0]], [[2qhm]], [[2qhn]], [[2r0u]], [[3f9n]], [[2wmq]], [[2wmr]], [[2wms]], [[2wmt]], [[2wmu]], [[2wmv]], [[2wmw]], [[2wmx]], [[2xey]], [[2xf0]], [[2xez]], [[2x8d]], [[2x8e]], [[2x8i]], [[2ydi]], [[2ydj]], [[2ydk]], [[2yer]], [[2yex]], [[2ym3]], [[2ym4]], [[2ym5]], [[2ym6]], [[2ym7]], [[2ym8]], [[2ywp]], [[3jvr]], [[3jvs]], [[3nlb]], [[3ot3]], [[3ot8]], [[3pa3]], [[3pa4]], [[3pa5]], [[3tkh]], [[3tki]], [[3u9n]], [[4fsm]], [[4fsn]], [[4fsq]], [[4fsr]], [[4fst]], [[4fsu]], [[4fsw]], [[4fsy]], [[4fsz]], [[4ft0]], [[4ft3]], [[4ft5]], [[4ft7]], [[4ft9]], [[4fta]], [[4ftc]], [[4fti]], [[4ftj]], [[4ftk]], [[4ftl]], [[4ftm]], [[4ftn]], [[4fto]], [[4ftq]], [[4ftr]], [[4ftt]], [[4ftu]], [[4gh2]], [[4hyh]], [[4hyi]], [[4jik]], [[4qye]], [[4qyf]], [[4qyg]], [[4qyh]], [[4rvk]], [[4rvl]], [[4rvm]], [[5dls]], [[5f4n]], [[5fcf]], [[5fck]], [[6fc8]], [[6fcf]], [[6fck]], [[7bko]], [[8e80]], [[8e81]] - hChk1 kinase domain + inhibitor 
**[[5oot]], [[5op2]], [[5op4]], [[5op5]], [[5op7]], [[5opb]], [[5opr]], [[5ops]], [[5opu]], [[5opv]], [[5oq5]], [[5oq6]], [[5oq7]], [[5oq8]], [[7bjd]], [[7bjh]], [[7bjj]], [[7bjm]], [[7bjo]], [[7bjr]], [[7bjx]], [[7bk1]], [[7bk2]], [[7bk3]], [[7mck]], [[7suf]], [[7sug]], [[7suh]], [[7sui]], [[7suj]], [[8siv]], [[8siw]], [[8six]] - hChk1 kinase domain (mutant) + inhibitor
**[[5oop]] - hChk1 kinase domain (mutant) + AMPPNP
**[[5oor]] - hChk1 kinase domain (mutant) + staurosporine
**[[7bkn]] - hChk1 kinase domain + adenine
**[[7bje]] - hChk1 kinase domain (mutant) + adenine
**[[2jqi]] – yChk1 – yeast
*'''Chk2 (Checkpoint kinase)'''
**[[1gxc]] – hChk2 phosphothreonine-binding domain + phosphopeptide
**[[2cn5]] – hChk2 kinase domain + ADP
**[[2cn8]] – hChk2 kinase domain + inhibitor
**[[2cn8]], [[2uv2]], [[2w0j]], [[2w7x]], [[2wtc]], [[2wtd]], [[2wti]], [[2wtj]], [[2xbj]], [[2xk9]], [[2xm8]], [[2xm9]], [[2ycf]], [[2ycq]], [[2ycr]], [[2ycs]], [[2yiq]], [[2yir]], [[2yit]], [[4a9r]], [[4a9s]], [[4a9t]], [[4bda]], [[4bdb]], [[4bdc]], [[4bdd]], [[4bde]], [[4bdf]], [[4bdg]], [[4bdh]], [[4bdi]], [[4bdj]], [[4bdk]] - hChk2 kinase domain + inhibitor
**[[3i6u]], [[3i6w]] – hChk2 residues 84-502 (mutant)
*'''Chk3 (Mst2)'''; domains - kinase 13-313; SARAH 436-484
**[[3wws]], [[4hkd]], [[4l0n]], [[4oh9]] – hChk3 SARAH domain 
**[[4lg4]] – hChk3 kinase domain
**[[4lgd]] – hChk3 kinase domain + RASSF5 SARAH domain
**[[6ao5]] – hChk3 kinase+SARAH domains (mutant) + SAV1 SARAH domain
**[[5dh3]], [[8a66]] – hChk3 kinase domain + inhibitor
*'''Chk4 (Mst1)''' ; Domains – kinase 1-311; SARAH 432-480
**[[3com]] – hChk4 kinase domain
**[[6yat]], [[8a5j]]– hChk4 kinase domain + inhibitor
**[[4nr2]] – hChk4 SARAH domain
**[[2jo8]] – hChk4 SARAH domain - NMR
**[[4oh8]] – hChk4 SARAH domain + Ras association domain-containing protein
*'''Chk5 (Aurora kinase b)'''
**[[4af3]] – hChk5 + inhibitor
*'''Chk6 or Chk15 or Aurora kinase A'''
**[[1mq4]], [[1muo]], [[4j8n]], [[4o0s]], [[6cpe]] – hChk6 kinase domain 
**[[4bn1]], [[4o0w]], [[4o0u]] – hChk6 kinase domain (mutant)
**[[5dnr]], [[5drd]], [[5dt3]] – hChk6 kinase domain + ATP
**[[5drd]] – hChk6 kinase domain + ATP
**[[1ol6]] – hChk6 kinase domain (mutant) + ATP
**[[2wqe]] – hChk6 kinase domain (mutant) + ADP
**[[5odt]] – hChk6 kinase domain (mutant) + ADP + TACC3
**[[2c6d]] – hChk6 kinase domain (mutant) + ADPNP
**[[2dwb]] – hChk6 kinase domain + AMPPNP
**[[6cpf]] – hChk6 kinase domain + AMPPCP
**[[5g15]] – hChk6 kinase domain + AMPPNP + monobody
**[[6cpg]], [[8ssp]] – hChk6 kinase domain + inhibitor + monobody
**[[2j4z]], [[2j50]], [[2np8]], [[2x81]], [[2x6d]], [[2x6e]], [[3efw]], [[3myg]], [[3vap]], [[3w10]], [[3w16]], [[3w18]], [[3w2c]], [[4b0g]], [[4byi]], [[4byj]], [[4j8m]], [[4jai]], [[4jaj]], [[4uyn]], [[4uzd]], [[4uzh]], [[4zs0]], [[4ztq]], [[4ztr]], [[4zts]], [[5aad]], [[5aae]], [[5aag]], [[5dpv]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5obr]], [[5one]], [[5zan]], [[6c2r]], [[6c2t]], [[6gra]], [[6z4y]], [[7ayh]], [[7ayi]], [[7fic]], [[7o2v]], [[8jmx]] – hChk6 kinase domain + inhibitor 
**[[2bmc]], [[2c6e]], [[2wtw]], [[2xne]], [[2xng]], [[2xru]], [[3coh]], [[3fdn]], [[3h0y]], [[3h0z]], [[3h10]], [[3lau]], [[3k5u]], [[3m11]], [[3nrm]], [[3p9j]], [[3r21]], [[3r22]], [[3qbn]], [[3unz]], [[3uo4]], [[3uo5]], [[3uo6]], [[3uod]], [[3uoh]], [[3uoj]], [[3uok]], [[3uol]], [[3up2]], [[3up7]], [[4dea]], [[4deb]], [[4ded]], [[4dee]], [[4dhf]], [[4jbo]], [[4jbp]], [[4jbq]], [[4prj]], [[5aad]], [[5aae]], [[5aaf]], [[5aag]], [[5dpv]], [[6hjj]], [[6hjk]] – hChk6 kinase domain (mutant) + inhibitor 
**[[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[5dos]], [[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5dn3]], [[5dos]], [[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[6c83]] – hChk6 kinase domain + AMPPCP + nanobody
**[[8sso]] – hChk6 kinase domain + drug + monobody
**[[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5g1x]], [[7ztl]] – hChk6 kinase domain (mutant) + N-Myc
**[[8guw]] – hChk6 kinase domain/activator peptide
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + Targeting protein for XKLP2
**[[3d14]], [[3d15]], [[3d2i]], [[3d2k]] [[3daj]], [[3dj5]], [[3dj6]], [[3dj7]] – Chk6 kinase domain (mutant) + inhibitor - mouse 
*Chk6 with phosphorylated Thr 287, Thr288
**[[1ol5]], [[1ol7]] – hChk6 kinase domain + PThr + ADP
**[[5dnr]], [[5dt3]] – hChk6 kinase domain + PThr + ATP
**[[2w1c]], [[2w1d]], [[2w1e]], [[2w1f]], [[2w1g]], [[5dn3]] – hChk6 kinase domain + PThr + inhibitor
**[[2wtv]], [[5orl]], [[5orn]], [[5oro]], [[5orp]], [[5orr]], [[5ors]], [[5ort]], [[5orv]], [[5orw]], [[5orx]], [[5ory]], [[5orz]], [[5os0]], [[5os1]], [[5os2]], [[5os3]], [[5os4]], [[5os5]], [[5os6]], [[5osd]], [[5ose]], [[5osf]] – hChk6 kinase domain (mutant) + PThr + inhibitor
**[[3e5a]], [[3ha6]] – hChk6 kinase domain + PThr + inhibitor + targeting protein for XKLP2
**[[5g1x]] – hChk6 kinase domain (mutant) + PThr + N-Myc
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + PThr + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + PThr + TPX2
**[[6r4a]], [[6r4b]], [[6r4c]], [[6r4d]] – hChk6 kinase domain + PThr + inhibitor + ADP
**[[6i2u]] – hChk6 kinase domain (mutant) + PThr + inhibitor + ADP
**[[6r49]] – hChk6 kinase domain (mutant) + PThr + CoA
*'''Chk10 (lymphocyte-oriented kinase)''' or LOK or STK10
**[[7qgp]] – hChk10
**[[2j7t]], [[4aot]], [[4equ]], [[4usd]], [[4use]], [[5ajq]], [[5owq]], [[5owr]], [[6eim]], [[6gtt]], [[6hxf]], [[6i2y]] – hChk10 kinase domain + inhibitor
**[[4bc6]], [[6i2y]] – hChk10 + drug
*'''Chk11'''
**[[2wtk]] – hChk11 (mutant) + calcium-binding protein
*'''Chk12-A (Aurora kinase b-a or Aurora B kinase)'''
**[[2vgo]], [[2vgp]], [[2vrx]], [[3ztx]], [[4c2v]], [[5eyk]] – fChk12-A + inner centromere protein A peptide + inhibitor - frog
**[[4c2w]] – fChk12-A + inner centromere protein A peptide + AMPPNP
**[[4b8l]], [[4b8m]], [[5k3y]] – fChk12-A (mutant) + inner centromere protein A peptide + inhibitor
*'''Chk13 (Polo-like kinase Plk)'''
*Plk1 Polo-box domain (Pbd) 371-594''
**[[1q4o]], [[2ogq]], [[3hih]], [[3p2w]], [[4h5x]], [[6n46]] – hPlk1 Pbd
*Plk1 Pbd complex with polypeptide
**[[1umw]], [[2ojx]], [[3bzi]], [[3c5l]], [[3rq7]], [[4dfw]], [[4rcp]], [[4o6w]], [[4o56]], [[4whh]], [[4whk]], [[4whl]], [[5dms]], [[5dmv]], [[5dnj]] , [[7mso]], [[7mx1]] – hPlk1 + peptide
**[[3hik]], [[3fvh]], [[3p2z]], [[3p34]], [[3p35]], [[3p36]], [[3p37]], [[3q1i]], [[4e67]], [[4e9c]], [[4e9d]], [[4hab]], [[4hy2]], [[4o9w]], [[4x9r]], [[4x9v]], [[4x9w]], [[5j19]], [[6gy2]] – hPlk1 + phosphopeptide
**[[1q4k]] – hPlk1 (mutant) + phosphopeptide
**[[2v5q]] – hPlk1 + design ankyrin repeat protein
**[[4lkl]] – hChk Plk1 + PL-55
**[[4lkm]] – hChk Plk1 + PL-74
**[[6ax4]] – hChk Plk1 + histidine cyclized macrocycle
**[[5x3s]] – mPlk1 + phosphopeptide
**[[8joq]], [[8joy]] – hPlk1 Pbd + hpv peptide
*Plk1 Pbd complex with small molecule inhibitor
**[[4h71]], [[4hco]], [[5ta6]], [[5ta8]], [[8bjt]], [[8crc]] – hPlk1 + inhibitor
**[[2rku]] – hPlk1 (mutant) + inhibitor
**[[3db6]], [[3db8]], [[3dbc]], [[3dbd]], [[3dbe]], [[3dbf]] – zfPlk1 (mutant) + inhibitor – zebra fish
*Plk1 catalytic domain 36-345
**[[2owb]] – hPlk1 catalytic domain (mutant)
**[[2ou7]] – hPlk1 catalytic domain (mutant) + AM
**[[2yac]], [[3kb7]], [[3thb]], [[4a4l]], [[4a4o]] – hPlk1 catalytic domain + inhibitor
**[[3fc2]] – hPlk1 catalytic domain (mutant) + inhibitor
**[[4j52]], [[4j53]] – hChk Plk1 (mutant) + inhibitor
**[[3d5x]] – zfPlk1 catalytic domain (mutant) + wortmannin
**[[3d5w]] – zfPlk1 catalytic domain + ADP
*'''Plk2'''
**[[4i5m]], [[4i5p]], [[4i6b]], [[4i6f]], [[4i6h]] – hChk Plk2 kinase domain (mutant) + inhibitor
**[[4rs6]], [[4xb0]] – hChk Plk2 Pbd
*'''Plk3'''
**[[4b6l]], [[4i6b]] – hChk Plk3 kinase domain + inhibitor
*'''Plk4'''; Domains – kinase 2-275; Pbd 580-808; Pb3 884-970
**[[3cok]] – hChk Plk4 kinase domain
**[[4n9j]] – hChk Plk4 Pbd domain
**[[4n7v]], [[4n7z]] – hChk Plk4 Pbd domain + centrosomal protein
**[[6w38]], [[6w3i]] – hChk Plk4 Pbd domain + Fam46C
**[[6w3j]] – hChk Plk4 Pbd domain + Fam46C + CEP92 peptide
**[[4jxf]], [[4yur]] – hChk Plk4 kinase domain + inhibitor
**[[5lhy]] – hChk Plk4 Pb3 domain
**[[4yyp]], [[5lhz]] – hChk Plk4 Pb3 domain + Scl-interrupting locus protein
**[[4g7n]], [[4nk7]], [[5lhx]], [[7rl3]] – DmChk Plk4 Pbd domain – ''Drosophila melanogaster''
*'''Chk16'''
**[[2buj]] – hChk16 (mutant) + staurosporin
*'''Chk17B''' or DRAK2 or STK17B
**[[3lm0]] – hChk17B
**[[6qf4]], [[7q7c]], [[7q7d]] – hChk17B + ADP
**[[7q7e]] – hChk17B + ATP
**[[3lm5]] – hChk17B + quercetin
**[[6y6f]], [[6y6h]], [[6zjf]] – hChk17B + pyrimidine derivative
**[[7akg]] – hChk17B + drug
*'''Chk19''' or STK19
**[[7xrb]] – hChk19
*'''Chk24 (Mst3)''' or STK24
**[[3a7f]], [[3a7g]], [[3a7h]], [[3a7i]], [[3a7j]], [[3ckw]] – hChk24 kinase domain
**[[4qmm]], [[4qmn]], [[4qmo]], [[4qmp]], [[4qmq]], [[4qms]], [[4qmt]], [[4qmu]], [[4qmv]], [[4qmw]], [[4qmx]], [[4qmy]], [[4qmz]], [[4qna]], [[4qo9]], [[4u8z]], [[4w8d]], [[4w8e]], [[7b30]], [[7b31]], [[7b32]], [[7b33]], [[7b34]], [[7b35]], [[8bzi]], [[8bzj]], [[8qlr]], [[8qls]], [[8qlt]] – hChk Mst3 + inhibitor
**[[8qlq]] – hChk Mst3 + macrocyclic inhibitor
**[[3ckx]] – hChk24 kinase domain + staurosporin
**[[3zhp]] – hChk24 kinase domain + calcium-binding protein
**[[4o27]] – hChk24 kinase domain (mutant) + calcium-binding protein
**[[4qml]] – hChk Mst3 kinase domain + AMPPNP
*'''Chk25 or STK25'''
**[[2xik]] – hChk25 kinase domain
**[[7z4v]] – hChk25 kinase domain + inhibitor
**[[3w8h]] – hChk25 regulatory domain + programmed cell death protein 10
**[[4nzw]] – hChk25 kinase domain (mutant) + calcium-binding protein
*'''Chk26 (Mst4)'''
**[[3ggf]], [[7b36]] – hChk Mst4 + inhibitor
**[[[3w8i]], [4geh]] - hChk Mst4 dimerization domain + programmed cell death protein 10
**[[4fza]], [[4fzd]], [[4fzf]] – hChk Mst4 (mutant) + calcium-binding protein
*'''Chk32'''
**[[4fr4]] – hChk32A
*'''Chk38'''
**[[6bxi]] – hChk38 kinase domain
*'''Chk39''' or SPAK
**[[7o86]] – hChk39 C-terminal
**[[5d9h]] – mChk39 residues 63-403 + ATP
**[[5dbx]] – mChk39 residues 63-403 (mutant) + AMPPNP
*'''Chk40'''
**[[5l2q]] – hChk40 kinase homology domain
*'''Dclk1'''
**[[6kyq]] – hChk Dclk1 kinase domain
**[[6kyr]] – hChk Dclk1 kinase domain (mutant)
**[[5jzj]] – hChk Dclk1 kinase domain + AMPPN
**[[5jzn]], [[7kx6]], [[7kxw]] – hChk Dclk1 kinase domain + inhibitor
**[[7f3g]] – hChk Dclk1 kinase domain + drug
**[[7kx8]] – hChk Dclk1 C-terminal + inhibitor
*'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123; kinase 144-480
**[[1unp]], [[1unr]] – hRac-α hChk pleckstrin homology domain
**[[2uzr]], [[2uzs]], [[7myx]] – hRac-α hChk pleckstrin homology domain (mutant)
**[[1h10]], [[1unq]], [[2uvm]] – hRac-α hChk pleckstrin homology domain + inositol tetrakisphosphate
**[[3o96]], [[4ejn]], [[6hhf]], [[6hhg]], [[6hhh]], [[6hhi]], [[6hhj]], [[6s9w]], [[6s9x]] - hRac-α hChk + inhibitor
**[[5kcv]], [[7nh4]], [[7nh5]] - hRac-α hChk (mutant) + inhibitor
**[[4ekl]], [[4gv1]] - hRac-α hChk kinase domain + inhibitor
**[[3qkm]], [[6ccy]] - hRac-α hChk kinase domain (mutant) + inhibitor
**[[6buu]] - hRac-α hChk kinase domain + bisubstrate peptide
**[[4ekk]] - hRac-α hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[6npz]] - hRac-α hChk kinase domain + peptide + inhibitor
**[[3ow4]], [[3qkk]], [[3qkl]], [[6buu]] - hRac-α hChk kinase domain (mutant) + peptide + inhibitor
**[[7apj]] - hRac-α hChk + nanobody
*'''Rac-β hChk (AKT2)'''
**[[1gzk]], [[1gzn]], [[1gzo]], [[1mrv]], [[1mry]] – hRac-β hChk kinase domain
**[[1p6s]] - hRac-β hChk pleckstrin homology domain - NMR
**[[1o6k]] - hRac-β hChk kinase domain + GSK3 peptide + AMPPNP
**[[2jdo]], [[2jdr]], [[2uw9]], [[2x39]], [[3cqu]], [[3cqw]] - hRac-β hChk kinase domain + GSK3 peptide + inhibitor
**[[3e87]], [[3e88]], [[3e8d]] - Rac-β hChk kinase domain (mutant) + GSK3 peptide + inhibitor<br /
**[[1o6l]] - hRac-β hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[3d0e]], [[8q61]] - hRac-β hChk kinase domain (mutant) + inhibitor
*'''Rac-γ hChk (ATK3)'''
**[[2x18]] – Rac-γ hChk PH domain
*'''A-Raf'''
**[[1wxm]] – hA-Raf RAS-binding domain 19-91 - NMR
**[[2mse]] – hA-Raf RAS-binding domain + APOA-I + K-ras - NMR
*'''B-Raf'''; domains - BRS 38-116; Ras-binding 153-237; kinase 445-723
**[[8dgs]], [[8dgt]] – hB-Raf in Ras/Raf complex – Cryo EM
**[[7z37]], [[7z38]], [[7zr5]] – hB-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
**[[1uwh]], [[3c4c]], [[6v2u]], [[6xfp]], [[6xlo]], [[8f7o]], [[8f7p]] – hB-Raf kinase domain + anticancer drug
**[[1uwj]], [[6p3d]] – hB-Raf kinase domain (mutant) + anticancer drug
**[[2fb8]], [[3d4q]], [[3e26]], [[3ii5]], [[3ppj]], [[3ppk]], [[3prf]], [[3pri]], [[3psb]], [[3psd]], [[3q4c]], [[3q96]], [[3skc]], [[3tv4]], [[3tv6]], [[4dbn]], [[4e26]], [[4e4x]], [[4ehe]], [[4fc0]], [[4g9c]], [[4h58]], [[4ksp]], [[4ksq]], [[4mbj]], [[4pp7]], [[6cad]], [[7shv]] – hB-Raf kinase domain + pyrazole inhibitor 
**[[3idp]], [[4ehg]], [[4fk3]], [[4g9r]], [[4jvg]], [[4mnf]], [[4r5y]], [[4rzv]], [[4rzw]], [[4wo5]], [[4xv1]], [[4xv2]], [[4xv3]], [[4xv9]], [[4yht]], [[5c9c]], [[5hi2]], [[5ita]], [[5jrq]], [[5jsm]], [[5jt2]], [[6nsq]], [[6p7d]], [[6uuo]] – hB-Raf kinase domain (mutant) + pyrazole inhibitor
**[[5csw]], [[5csx]], [[5ct7]], [[5fd2]], [[5hid]], [[5hie]], [[5val]], [[5vam]], [[6b8u]], [[6n0p]], [[6n0q]], [[7k0v]], [[7p3b]], [[7p3v]], [[8c7x]], [[8c7y]] - hB-Raf kinase domain + inhibitor
**[[6v34]] – hB-Raf kinase domain (mutant) + inhibitor
**[[4mne]] – hB-Raf kinase domain + MAPKK1
**[[8f7o]] – hB-Raf kinase domain + drug
**[[7m0u]] – hB-Raf kinase domain + AMPPNP + drug
**[[6u2h]] – hB-Raf kinase domain + 14-3-3 ζ/δ
**[[7mfe]] – hB-Raf + 14-3-3 ζ/δ – Cryo EM
**[[7mff]] – hB-Raf + 14-3-3 ζ/δ + inhibitor – Cryo EM
**[[7mfd]] – hB-Raf + 14-3-3 ζ/δ + MEK + inhibitor – Cryo EM
**[[6pp9]] – hB-Raf kinase domain + MEK1 + ANP
**[[7m0x]], [[7m0z]] – hB-Raf kinase domain + MEK1 + ANP + inhibitor
**[[7m0t]], [[7m0u]], [[7m0v]], [[7m0w]], [[7m0y]] – hB-Raf kinase domain + MEK1 + ANP + drug
**[[6u2g]] – hB-Raf kinase domain + MEK1 + AMPPCP
**[[5vr3]] – hB-Raf BRS domain
**[[7jhp]] – hB-Raf BRS domain + Hras
**[[6ntc]], [[6ntd]] – hB-Raf BRS domain (mutant) + Hras
**[[6xi7]] – hB-Raf 52-188 + Kras
**[[2l05]], [[5j17]], [[5j2r]] – hB-Raf RAS-binding domain - NMR
**[[3ny5]] – hB-Raf RAS-binding domain
**[[5j18]] – hB-Raf RAS-binding domain + inhibitor - NMR
**[[6pts]], [[6ptw]] – hB-Raf 56-187 + Kras + apolipoprotein + GMPPNP - NMR
**[[6q0k]], [[6uan]] – hB-Raf + 14-3-3 ζ – Cryo EM
**[[6nyb]] – hB-Raf + 14-3-3 ζ + MEK1 – Cryo EM
**[[6q0t]], [[6q0j]] – hB-Raf (mutant) + 14-3-3 ζ + MEK1 – Cryo EM
*'''c-Raf'''; Domains – RAS-binding (RBD) 55-132; Cys-rich 136-187 (CBD); kinase 323-618
**[[1rfa]], [[8jna]], [[8jof]], [[8jog]] – hc-Raf RBD - NMR
**[[1faq]], [[1far]] – hc-Raf cysteine-rich domain - NMR
**[[3omv]] – hc-Raf kinase domain
**[[1rrb]] – c-Raf RBD – NMR - rat
*c-Raf complex with protein
**[[8cpd]] – hc-Raf + 14-3-3 protein zeta – Cryo EM
**[[9mmp]] – hc-Raf + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[9mmr]] – hc-Raf (mutant) + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[1c1y]] – hc-Raf RBD + RAP1A
**[[3kuc]] – hc-Raf RBD (mutant) + RAP1A
**[[1gua]] – hc-Raf RBD + RAP1A + GPPNHP
**[[8jnb]] – hc-Raf RBD + ligand
**[[4g0n]], [[4g3x]] – hc-Raf RBD + GTPase Hras
**[[3kud]] – hc-Raf RBD (mutant) + GTPase Hras
**[[8epw]], [[8t74]] – hc-Raf RBD + GTPase K-ras
**[[8t75]], [[9ygs]] – hc-Raf RBD-CRD + GTPase K-ras + GMPPNP
**[[9ay7]], [[9aya]] – hc-Raf + MEK1
**[[9mmq]] – hc-Raf + MEK1 – Cryo EM
**[[9mms]] – hc-Raf (mutant) + MEK1 – Cryo EM
**[[9o0u]], [[9o0v]] – hc-Raf (mutant) + MEK1 + ANP + inhibitor– Cryo EM
**[[8u1l]] – hc-Raf + Hsp90 + CDC37 – Cryo EM
**[[8gae]], [[8gft]] – hc-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
*'''Snf1-related Chk'''
**[[3uc4]], [[3uc3]], [[3udb]], [[3zut]], [[3zuu]] – AtChk Srk2E kinase domain (mutant) – ''Arabidopsis thaliana''
**[[3ujg]] – AtChk Srk2E kinase domain (mutant) + protein phosphatase 2C
**[[5yks]] – hChk
*'''MAPK-interacting Chk''' or Mnk1 Mnk2
**[[2hw6]] – hMnk 1 catalytic domain
**[[2hw7]] – hMnk 1 catalytic domain + staurosporin
**[[5wvd]] – hMnk 1 catalytic domain + inhibitor
**[[2ac3]] – hMnk 2 catalytic domain
**[[2ac5]] – hMnk 2 catalytic domain (mutant)
**[[6cj5]], [[6cje]], [[6cjh]], [[6cjw]], [[6cjy]], [[6ck3]], [[6ck6]], [[6cki]] – hMnk 2 catalytic domain (mutant) + inhibitor
*'''hChk Pak''' or '''Chk N''' or '''PRK1'''; Domains - CRIB 74-109; Hr1B 122-199; catalytic 109-426; kinase 605-942
**[[1urf]] – hChk Pak-1 Hr1b domain - NMR
**[[4nkg]] – hChk Pak-1 Hr1b domain + SSPH1 LRR domain
**[[2rmk]] – hChk Pak-1 Hr1bb domain + Rac1 - NMR
**[[1f3m]] – hChk Pak-1 autoregulatory+kinase domains
**[[4otd]] - hChk Pak-1 kinase domain
**[[1yhv]], [[1yhw]], [[3q4z]], [[3q52]], [[3q53]] – hChk Pak-1 kinase domain (mutant)
**[[4o0r]], [[4o0t]], [[4zji]], [[4zjj]], [[4zlo]], [[4zy4]], [[4zy5]], [[4zy7]], [[5ime]], [[5kbq]], [[5kbr]], [[6b16]], [[7vto]] – hChk Pak-1 kinase domain + inhibitor
**[[4oti]], [[4oth]], [[4otg]] – hChk Pak-1 kinase domain + inhibitor
**[[4eqc]], [[4p90]], [[5dew]], [[5dey]], [[5dfp]] – hChk Pak-1 kinase domain (mutant) + inhibitor
**[[2hy8]] – hChk Pak-1 kinase domain + staurosporin
**[[2qme]] – hChk Pak-1 CRIB domain + RAC3
**[[3fxz]], [[3fy0]], [[4daw]] – hChk Pak-1 kinase domain (mutant) + Ru complex
**[[6fd3]] – hChk Pak-3 kinase domain (mutant)
**[[2j0i]], [[4fie]] – hChk Pak-4
**[[4fig]], [[4fij]], [[4l67]] – hChk Pak-4 kinase domain
**[[2cdz]] – hChk Pak-4 + purine derivative
**[[2ov2]] – hChk Pak-4 CRIB domain + RAC3
**[[2qon]], [[4fif]], [[4fih]], [[4fii]], [[4jdh]], [[4jdi]], [[4jdj]], [[4jdk]], [[6wlx]], [[6wly]] – hChk Pak-4 kinase domain + peptide
**[[4app]], [[4njd]], [[4o0v]], [[4o0x]], [[4o0y]], [[4xbu]], [[5bms]], [[5i0b]], [[5vee]], [[5vef]], [[5xva]], [[5xvf]], [[5xvg]], [[5zjw]], [[7cmb]], [[7cp3]], [[7cp4]] – hChk Pak-4 kinase domain + inhibitor
**[[2x4z]], [[2xh5]] – hChk Pak-4 kinase domain (mutant) + inhibitor
**[[5upk]], [[5upl]] – hChk Pak-4 kinase domain (mutant) + CDC42
**[[5ved]] – hChk Pak-4 kinase domain + staurosporine
**[[8ahi]] – hChk Pak-4 300-591 + inhibitor
**[[7s46]], [[7s48]] – hChk Pak-4 catalytic domain + integrin beta-5 peptide
**[[2c30]] – hChk Pak-6
**[[2odb]] – hChk Pak-6 CRIB domain + CDC42
**[[4ks8]] – hChk Pak-6 kinase domain + sunitinib
**[[4ks7]] – hChk Pak-6 kinase domain (mutant) + inhibitor
**[[2f57]] – hChk Pak-7
*'''Mycobacterium tuberculosis Chk Pkn'''
**[[4x3f]] - MtChk PknA – ''Mycobacterium tuberculosis''
**[[4ow8]] - MtChk PknA kinase domain
**[[3ori]], [[3ork]], [[3orl]], [[3orm]], [[3oro]], [[3orp]], [[3ort]] - MtChk PknB kinase domain (mutant)
**[[1o6y]] – MtChk PknB kinase domain
**[[6b2p]], [[6b2q]] – MtChk PknB kinase domain + inhibitor
**[[2kud]], [[2kue]], [[2kuf]], [[2kui]] – MtChk PknB pasta domains 2-3 - NMR
**[[3ouv]] – MtChk PknB pasta domain 3
**[[5e0y]] – MtChk PknB pasta domain 4
**[[5e10]] – MtChk PknB pasta domains 1-2
**[[5e0z]] – MtChk PknB pasta domains 3-4
**[[5e12]] – MtChk PknB pasta domains 2-4
**[[5u94]] - MtChk PknB kinase domain + inhibitor
**[[3f61]], [[3f69]] - MtChk PknB kinase domain (mutant) + inhibitor
**[[6i2p]] - MtChk PknB kinase domain (mutant) + GARA + peptide
**[[1rwi]], [[1rwl]] - MtChk PknD extracellular domain
**[[2h34]] – MtChk PknE catalytic domain
**[[7naa]] – MtChk PknF kinase domain + inhibitor
**[[4y12]] - MtChk PknG + ATP-gS
**[[4y0x]] - MtChk PknG + ADP
**[[7q52]] - MtChk PknG + inhibitor
**[[4esq]] - MtChk PknH extracellular domain
**[[5m06]], [[5xka]] - MtChk PknI kinase domain
**[[5m07]], [[5m08]], [[5m09]] - MtChk PknI kinase domain (mutant)
**[[5xll]], [[5xlm]] - MtChk PknI sensor domain
**[[7mxb]], [[7mxj]], [[7mxk]] - Chk PknG kinase domain + AMPPNP - Corynebacterium glutamicum
*'''hChk Nek'''
**[[4apc]] – hChk Nek1 kinase domain (mutant)
**[[4b9d]] - hChk Nek1 kinase domain (mutant) + inhibitor
**[[2w5h]] – hChk Nek2 kinase domain
**[[2jav]], [[2wqo]], [[2xk3]], [[2xk4]], [[2xk6]], [[2xk7]], [[2xk8]], [[2xkc]], [[2xkd]], [[2xke]], [[2xkf]], [[2xnm]], [[2xnn]], [[2xno]], [[2xnp]], [[4a4x]], [[4afe]], [[5m51]], [[5m53]], [[5m55]], [[5m57]], [[6sgd]], [[6sgh]], [[6sgi]], [[6sgk]], [[6sk9]] – hChk Nek2 + inhibitor
**[[2w5a]], [[2w5b]] – hChk Nek2 + nucleotide
**[[6tm5]] - hChk Nek2 in anaphase-promoting complex – Cryo EM
**[[2wqm]], [[6s76]] – hChk Nek7
**[[2wqn]] – hChk Nek7 + ADP
**[[5de2]] – hChk Nek7 + hChk Nek9
**[[2wqo]], [[6s73]] – hChk Nek7 + inhibitor
**[[6npy]] – hChk Nek7 + Nlrp3
**[[6s75]] – hChk Nek7 + inhibitor
*'''Chk Rio'''
**[[6fdm]], [[6fdn]], [[6fdo]] – hChk Rio2
**[[4otp]] – hChk Rio1 Rio domain + ADP
**[[6hk6]], [[7vbt]] – hChk Rio2 + inhibitor
**[[6eml]], [[6fai]], [[6g18]], [[6g51]], [[6rbd]],[[6rbe]], [[6y7c]] – yChk Rio2 in 40S particle – Cryo EM
**[[1ztf]] – AfChk Rio1 + adenine derivative – Archaeoglobus fulgidus
**[[1zth]] – AfChk Rio1 + ADP
**[[1zp9]] – AfChk Rio1 + ATP
**[[1tqp]], [[1zao]] – AfChk Rio2 + ATP
**[[1zar]] – AfChk Rio2 + ADP
**[[4gyg]] – CtChk Rio2 – Chaetonium thermophilum
**[[4gyi]] – CtChk Rio2 + ADP
*hChk Vrk (vaccinia-related kinase)
**[[2kty]], [[2kul]], [[2lav]], [[2rsv]] – hChk Vrk1 kinase domain 1-396 - NMR
**[[3op5]] – hChk Vrk1 kinase domain (mutant)
**[[5ukf]] – hChk Vrk1 kinase domain + inhibitor
**[[5uvf]], [[6bu6]], [[6cfm]], [[6cnx]], [[6bp0]], [[6bru]], [[6btw]], [[6cmm]], [[6cqh]], [[6csw]], [[6dd4]], [[6npn]], [[6vxu]], [[6vzh]] – hChk Vrk1 kinase domain (mutant) + inhibitor
**[[6ac9]] – hChk Vrk1 kinase domain (mutant) + AMPPNP
**[[7tan]] – hChk Vrk1 kinase domain + nucleosome – Cryo EM
**[[2v62]] – hChk Vrk2 kinase domain
**[[5uu1]], [[6ncg]], [[8q1z]] – hChk Vrk2 kinase domain + inhibitor
*Chk Wnk (protein kinase lysine-deficient); Domains - kinase 194-483; CCT1 454-549
**[[4q2a]], [[4pwn]], [[6cn9]] - hChk Wnk1 kinase domain (mutant)
**[[5tf9]] - hChk Wnk1 kinase domain + inhibitor + AMPPNP
**[[5wdy]], [[5we8]] - hChk Wnk1 kinase domain + inhibitor + ANP
**[[5drb]], [[6ol2]]- rChk Wnk1 kinase domain (mutant) + inhibitor
**[[6elm]] - hChk Wnk2 CCT1 domain
**[[6fbk]] - hChk Wnk2 CCT1 domain + Wnk1 peptide
**[[5o1v]], [[5o21]], [[5o23]] - hChk Wnk3 kinase domain
**[[5o2c]] - hChk Wnk3 kinase + CCT1 domains
**[[5o26]], [[5tf9]] - hChk Wnk3 kinase domain + AMPPNP
**[[5o2b]] - hChk Wnk3 kinase domain + inhibitor
**[[8edh]] - hChk Wnk3 kinase domain (mutant) + inhibitor
**[[2lru]] – rChk Wnk1 autoinhibitory domain 480-572 - NMR
**[[5w7t]] - rChk Wnk1 kinase domain
**[[7uos]] - rChk Wnk1 kinase domain (mutant)
*'''TANK-binding kinase'''
**[[4efo]] – hChk Tbk1 ubiquitin-like domain
**[[6rsr]], [[6rsu]] – hChk Tbk1 + inhibitor
**[[4im0]], [[4im2]], [[4im3]], [[4ipq]], [[4iw0]], [[4iwo]], [[4iwp]], [[6rst]] – hChk Tbk1 (mutant) + inhibitor
**[[6cq5]], [[6cq4]], [[6cq0]], [[6boe]], [[6bod]], [[6bny]], [[5w5v]] – hChk Tbk1 + ulcer drug
**[[4eut]], [[4euu]] – hChk Tbk1 kinase+ubiquitin-like domains (mutant) + inhibitor
**[[6nt9]] – hChk Tbk1 (mutant) + STING
**[[5eoa]], [[5eof]] – hChk Tbk1 residues 677-729 + optineurin
**[[4jl9]], [[4jlc]] – mChk Tbk1 + inhibitor
**[[6o8b]], [[6o8c]] – mChk Tbk1 (mutant) + STING
*'''Haspin'''
**[[2vuw]], [[2wb8]] – hChk Haspin kinase domain
**[[3dle]] – hChk Haspin kinase domain + AMP
**[[3e7v]], [[3f2n]], [[3fmd]], [[3iq7]], [[4qtc]], [[5htb]], [[5htc]], [[6z56]], [[6z57]], [[6z58]], [[6z59]], [[6z5a]], [[6z5b]], [[6z5c]]. [[6z5d]], [[6z5e]] , [[7avq]], [[7ops]] – hChk Haspin kinase domain + inhibitor
**[[7sqm]] – hChk Haspin kinase domain + antimalarial
**[[6g34]], [[6g35]], [[6g36]], [[6g37]], [[6g38]] – hChk Haspin kinase domain + tubercidin derivative
**[[6g39]], [[6g3a]] – hChk Haspin kinase domain (mutant) + tubercidin derivative
**[[4ouc]] – hChk Haspin kinase domain + histone H3 peptide
*'''MAP/microtubule affinity-regulating kinase (MARK)'''
**[[2hak]] – hChk MARK1 catalytic+UBA domains
**[[3ose]] - hChk MARK1 KA1 domain
**[[6c9d]] – hChk MARK1 catalytic+UBA+KA1 domains (mutant)
**[[5eak]], [[5kz7]], [[5kz8]] – hChk MARK2 catalytic+UBA domains + inhibitor
**[[3iec]] – hChk MARK2 catalytic+UBA domains + cytotoxicity-associated immunodominant antigen peptide
**[[2qnj]] – hChk MARK3 catalytic+UBA domains
**[[3fe3]] – hChk MARK3 catalytic+UBA domains (mutant)
**[[7p1l]] – hChk MARK3 catalytic+UBA domains + inhibitor
**[[5es1]] – hChk MARK4 catalytic+UBA domains + inhibitor
**[[1zmu]] – rChk MARK2 catalytic+UBA domains
**[[2wzj]], [[2r0i]], [[1zmv]], [[1y8g]], [[1zmw]] – rChk MARK2 catalytic+UBA domains (mutant)
**[[1ul7]], [[1v5s]] - mChk MARK3 catalytic domain - NMR
*'''Mitotic checkpoint Chk (Bub)'''; Domains: TPR 1-220; kinase 726-1085
**[[2lah]] – hChk Bub1 TPR domain – NMR
**[[2wvi]] – hChk Bub1β TPR domain
**[[3si5]] – hChk Bub1 TPR domain + CASC5 peptide
**[[4qpm]], [[4r8q]], [[5dmz]] – hChk Bub1 kinase domain + ADP
**[[6f7b]] – hChk Bub1 kinase domain + inhibitor
**[[4a1g]] – hChk Bub1 TPR domain + CASC5 KI motif
**[[4ggd]] - hChk Bub1 + cell division cycle protein
**[[5khu]], [[6tlj]] - hChk Bub1 in anaphase-promoting complex – Cryo EM
**[[6jkk]] – DmChk Bub1 kinase domain
**[[6jkm]] – DmChk Bub1 kinase domain + ADP
**[[5jja]] – hChk Bub1 residues 661-734 + PP2A
**[[3esl]] – yChk Bub1 N terminal
**[[4bl0]] - yChk Bub1 + cell cycle arrest protein Bub3
*'''Microtubule-associated Chk'''
**[[2m9x]] – hChk 1 residues 187-287 – NMR
**[[3ps4]] - hChk 1 residues 965-1057
**[[2kqf]], [[2kyl]] – hChk 2 PDZ domain + glycoprotein C terminal – NMR
**[[3khf]] - hChk 3 PDZ domain
**[[2w7r]] – hChk 4 PDZ domain
*'''mTOR''' or '''Mechanistic target of rapamycin'''
*''mTOR FRB domain residues 2015-2114''
**[[1fap]], [[1nsq]] – hFRAP FRB domain + FKBP
**[[2rse]] – hFRAP FRB domain + FKBP – NMR
**[[1aue]] – hFRAP FRB domain
**[[2gaq]], [[2npu]] – hFRAP FRB domain - NMR
**[[8ppz]] – hFRAP FRB domain + FKBP + pyridine derivative
**[[2fap]], [[3fap]], [[4fap]] – hFRAP FRB domain + FKBP + rapamycin analog
**[[4drh]], [[4dri]], [[4drj]], [[5gpg]] – hFRAP FRB domain + FKBP + rapamycin
**[[6m4u]], [[6m4w]] – hChk Mtor FRB domain (mutant) + FKBP1A + rapamycin
**[[5wbh]] – hFRAP FRB domain + S6K1 peptide
*''mTOR FAT+PIKK domain residues 1376-2549''
**[[4jsn]] – hFRAP + TORC subunit LST8
**[[4jsp]] – hFRAP + TORC subunit LST8 + ATP
**[[4jsv]] – hFRAP + TORC subunit LST8 + ADP
**[[4jsx]] – hFRAP + TORC subunit LST8 + torin2
**[[4jt5]] – hFRAP + TORC subunit LST8 + pp242
**[[4jt6]] – hFRAP + TORC subunit LST8 + PI-103
**[[5wbu]], [[5wby]] – hFRAP + TORC subunit LST8 + proline-rich Akt1 substrate
*''mTOR complex''
**[[5flc]] – hmTOR + RAPTOR + LST8 + FKBP – Cryo EM
**[[5h64]] – hmTOR + RAPTOR + LST8 – Cryo EM
**[[6sb2]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC – Cryo EM
**[[6sb0]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC + proline-rich Akt1 substrate – Cryo EM
**[[5zcs]] – hmTOR + LST8 + AVO3 + TORC2 – Cryo EM
**[[7tzo]] – hTORC2 in mTORC2 complex– Cryo EM
**[[6zwm]], [[6zwo]], [[7owg]], [[7pe7]], [[7pe8]], [[7pe9]], [[7pea]], [[7peb]], [[7pec]], [[7uxc]] , [[8era]]– mTOR in mTor complex – Cryo EM
*'''Gcn2'''
**[[1zyc]] – yChk Gcn2
**[[1zxe]], [[1zy4]], [[1zy5]] – yChk Gcn2 (mutant)
**[[2yz0]] – yChk Gcn2 RWD/GI domain – NMR
**[[4otm]] – yChk Gcn2 C terminal domain
**[[1zyd]] – yChk Gcn2 + ATP
**[[4otn]] – mChk Gcn2 C terminal domain
*'''LRRK1''' or leucine-rich repeat Chk1
**[[8e04]], [[8e05]], [[8e06]], [[8fac]] – hLRRK1 – Cryo EM
*'''LRRK2''' or leucine-rich repeat Chk2 or dardarin
**[[6xr4]] – hLRRK2 – Cryo EM
**[[7lht]], [[7lhw]], [[7li4]] – hLRRK2 + ATP + GDP – Cryo EM
**[[7li3]] – hLRRK2 (mutant) + ATP + GDP – Cryo EM
**[[6oje]], [[7thy]] – hLRRK2 GTPase domain 1329-1520
**[[6ojf]] – hLRRK2 GTPase domain (mutant)
**[[6dlo]], [[6dlp]] – hLRRK2 WD40 domain
**[[7thz]] – hLRRK2 1330-1527 + GDP
**[[6vno]], [[6vp6]], [[6vp7]] – hLRRK2 C terminal 1330-2527 – Cryo EM
**[[6vp8]] – hLRRK2 C terminal 1330-2527 + COR domain 1670-1950 + WD40 domain 2140-2489 – Cryo EM
**[[6s6q]] – AtLRRK2 ectodomain + protein casparian strip peptide
*'''Pim'''
*Pim1 catalytic domain residues 14-313
**[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain
**[[1yxs]] – hPim1 catalytic domain (mutant)
**[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP
**[[1yxu]] – hPim1 catalytic domain + AMP
**[[1yxv]], [[5ipj]] – hPim1 catalytic domain + quinoline derivative
**[[1yxx]] – hPim1 catalytic domain + indole derivative
**[[2bzh]], [[2bzi]], [[2bzj]] – hPim1 catalytic domain (mutant) + organometallic ligand
**[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3c4e]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umw]], [[3umx]], [[4enx]], [[4eny]], [[4k0y]], [[4k18]], [[4k1b]], [[4i41]], [[4iaa]], [[4ll5]], [[4lm5]], [[4lmu]], [[4mbi]], [[4mbl]], [[4med]], [[4mta]], [[4n6y]], [[4n6z]], [[4n70]], [[4xh6]], [[5iis]], [[5kgd]], [[5kge]], [[5kgg]], [[5kgi]], [[5kgk]], [[5kzi]], [[5vua]], [[5vub]], [[5vuc]], [[6mt0]], [[6vrv]], [[7oov]], [[7oow]], [[7oox]], [[7xsv]] – hPim1 catalytic domain + inhibitor
**[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor
*Pim1 kinase domain residues 92-404
**[[4jx3]] – hPim1 kinase domain
**[[3uix]], [[5c1q]] – hPim1 kinase domain residues 120-404 + quinoline derivative
**[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate
**[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand
**[[1xws]], [[4alu]], [[4alv]], [[4alw]], [[4as0]], [[4bzn]], [[4bzo]], [[4dtk]], [[4jx7]], [[4rbl]], [[4rc2]], [[4rc3]], [[4rc4]], [[4ty1]], [[4wrs]], [[4wsy]], [[4wt6]], [[4xhk]], [[5dgz]], [[5dhj]], [[5dia]], [[5dwr]], [[5eol]], [[5kcx]], [[5o11]], [[5o12]], [[5o13]], [[5tel]], [[5tex]], [[5toe]], [[5v80]], [[5v82]]. [[6bsk]], [[6kzi]], [[6l11]], [[6l12]], [[6l13]], [[6l14]], [[6l15]], [[6l16]], [[6l17]], [[6no8]], [[6no9]], [[6vru]], [[6ykd]], [[7zun]] – hPim1 kinase domain + inhibitor
**[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor
*Pim1 full length
**[[4rpv]], [[5tur]] - hPim1 + inhibitor
*Pim1 complex with consensus peptide (pimtide)
**[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]], [[6qxk]] – hPim1 kinase domain + inhibitor + consensus peptide
**[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide
**[[2c3i]], [[5mzl]], [[5n4n]], [[5n4o]], [[5n4r]], [[5n4u]], [[5n4v]], [[5n4x]], [[5n4y]], [[5n4z]], [[5n50]], [[5n51]], [[5n52]], [[5n5l]], [[5n5m]], [[5ndt]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide
**[[4gw8]], [[7qb2]], [[7qfm]], [[7z6u]], [[8afr]] – hPim1 catalytic domain (mutant) + inhibitor + pimtide
**[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide
**[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide
*Pim1 containing phosphorylated Ser 261
**[[1yhs]] – hPim1 kinase domain + PSer + staurosporine
**[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor
**[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor
**[[1yi4]] – hPim1 kinase domain + PSer + adenosine
*Pim2
**[[4x7q]] – hPim2 catalytic domain + inhibitor
**[[2iwi]] – hPim2 catalytic domain + Ru ligand
*'''Rip or receptor-interacting Chk; Domains – catalytic 1-294; Amyloid fibril 418-518; Death 561-671'''
**[[6ac5]] – hRip1 death domain
**[[5tx5]], [[6c3e]], [[6c4d]], [[6nw2]], [[6r5f]], [[7fcz]], [[7fd0]], [[7ydx]] – hRip1 catalytic domain + inhibitor
**[[6hho]], [[6nyh]], [[6ocq]], [[6rln]] – hRip1 catalytic domain (mutant) + inhibitor
**[[6ggs]] – hRip2 – Cryo EM
**[[5yrn]] – hRip2 CARD domain 434-540 – Cryo EM
**[[5w5j]], [[5w5o]], [[6es0]], [[6fu5]], [[6hmx]], [[6rn8]], [[6rna]], [[6s1f]], [[6sze]], [[6szj]] – hRip2 catalytic domain + inhibitor
**[[6ul8]] – hRip2 catalytic domain (mutant) + inhibitor
**[[8aza]] – hRip2 catalytic domain + XiaP Bir2 domain – Cryo EM
**[[7mx3]] – hRip3 catalytic domain (mutant) + inhibitor
**[[7mon]] – hRip3 catalytic domain (mutant) + MLKL
**[[7dac]] – hRip3 amyloid fibril - NMR
**[[7da4]] – hRip3 amyloid fibril – Cryo EM
**[[6oko]] – mRip3 catalytic domain + inhibitor
**[[6jpd]] – mRip3 residues 409-486 - NMR
**[[5wnj]], [[5wnm]] – mRip4 catalytic domain (mutant) + drug
**[[5wnl]] – mRip4 catalytic domain (mutant) + staurosporine
**[[5wnk]] – mRip4 catalytic domain (mutant) + inhibitor
**[[5wni]] – mRip4 catalytic domain (mutant) + ATP
**[[6gwm]] – rRip2 caspase recruitment domain 433-539
*'''Ulk'''
**[[6qas]] – hChk Ulk1 + inhibitor
**[[5ci7]], [[6mnh]] – hChk Ulk1 (mutant) + inhibitor
**[[4wno]], [[4wnp]] – hChk Ulk1 + IST1 homolog
**[[8soi]], [[8sqz]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein
**[[8srm]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein – Cryo EM
**[[8srq]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein + PI3K – Cryo EM
**[[6qav]], [[6qau]], [[6qat]], [[6yid]] – hChk Ulk2 + inhibitor
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[6fdz]], [[6fdy]] – hChk Ulk3 + leukemia drug
**[[6tsz]] – hChk Ulk4 pseudfokinase domain + ATPgS
**[[6u5l]] – hChk Ulk4 (mutant) + inhibitor
*'''Hipa''' and '''Hipb'''
**[[3tpd]], [[3tpe]] – EcChk Hipa – ''Escherichia coli''
**[[3dnt]], [[3dnu]], [[3tpb]] – EcChk Hipa (mutant)
**[[4pu7]], [[4pu8]] – SoChk Hipb - ''Shewanella oneidensis''
**[[3tpt]] – EcChk Hipa (mutant) + ADP
**[[3fbr]] – EcChk Hipa (mutant) + AMPPNP + peptide
**[[3tpv]] – EcChk Hipa + ADP
**[[2wiu]] – EcChk Hipa + Hipb
**[[3dnv]], [[3hzi]], [[4yg7]], [[5k98]] – EcChk Hipa + Hipb + DNA
**[[4yg1]], [[4z58]], [[4z59]], [[4z5c]], [[4z5d]] – EcChk Hipb + DNA
**[[4z5h]] – EcChk Hipb (mutant) + DNA
**[[4pu3]], [[4pu4]] – SoChk Hipa + Hipb + DNA - ''Shewanella oneidensis''
**[[4pu5]] – SoChk Hipa + AMPPNP
*'''Chk Smg'''
**[[6l53]] – hChk Smg1 – Cryo EM
**[[7pw6]] – hChk Smg1 + inhibitor – Cryo EM
**[[7pw7]] – hChk Smg1 + Smg9 + inhibitor – Cryo EM
**[[7pw9]] – hChk Smg1 + Smg9 + AMPPNP + ATP – Cryo EM
**[[6l54]], [[6syt]] – hChk Smg1 + Smg8 + Smg9 – Cryo EM
**[[7pw4]], [[7pw5]] – hChk Smg1 + Smg8 + Smg9 + inhibitor – Cryo EM
**[[7pw8]] – hChk Smg1 + Smg8 + Smg9 + AMPPNP – Cryo EM
**[[6z3r]] – hChk Smg1 + Smg8 + Smg9 + regulator of nonsense transcripts – Cryo EM
**[[2hwy]] – hChk Smg5 PIN domain
**[[2hww]], [[2hwx]] – hChk Smg6 PIN domain (mutant)
**[[4um2]] – hChk Smg6 TPR domain
**[[1ya0]] – hChk Smg7 N terminal
*'''Chk Vprbp or DCAF1'''
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain 1039-1401 (mutant)
**[[7sse]], [[7ufv]], [[8f8e]], [[8og5]], [[8og6]], [[8og7]], [[8og8]], [[8og9]], [[8oga]], [[8ogb]], [[8ogc]], [[8oo5]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) + inhibitor
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[5aja]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
*'''Other Chk'''
**[[1wak]] – hChk Sprk1
**[[3dak]] – hChk Osr1 kinase domain
**[[7okw]] – hChk Osr1 C-terminal
**[[4aw2]] – hChk Mrckα kinase domain
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain (mutant)
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[1uf0]] – hChk Dcamkl1 DCX domain – NMR
**[[1u5q]] – rChk Tao2 kinase domain
**[[2cos]] – mChk Lats2 – NMR
**[[1xte]], [[1xtn]], [[6edx]] – mChk Sgk3 PX domain
**[[4yom]] – mChk Brsk2
**[[4ynz]] – mChk Brsk1 N terminal domain
**[[5iri]] – mChk Brsk1 residues 592-719
**[[5oat]], [[7mp8]] – rfbChk Pink1– red flour beetle
**[[7t3x]] – Chk Pink1 (mutant) – louse
**[[4f0g]] – smChk Roco4 kinase domain – slime mold
**[[5tos]] – AtChk Bik1
**[[1q8z]], [[1zyc]] – yChk
**[[1how]], [[1zxe]], [[1zy4]] – yChk (mutant)
**[[1ow5]], [[1x9x]] – yChk Ste11 SAM domain – NMR
**[[1w1n]], [[2kio]], [[2kit]] – yChk Tor1 FATC domain – NMR
**[[3gre]] – yChk Vps15 WD repeat domain
**[[3osm]], [[3ost]] - yChk Kcc4 kinase domain
**[[5yyx]] – yChk Mek1 FHA domain
**[[6jxa]], [[6jxc]] – yChk Tel1 – Cryo EM
**[[6u69]] – CaChk Yck2 – ''Candida albicans''
**[[6sky]], [[6skz]], [[6sl0]], [[6sl1]] – Chk Tel1 – ''Chaetonium thermophilum'' – Cryo EM
**[[6ra0]] – CeChk Dkf1 – ''Chaenorhabditis elegans''
**[[7z6e]] – CeChk Mrck1 regulatory domain
**[[6tlb]] – Chk – ''Plasmodium falciparum''
*Other Chk complexes
**[[1wbp]], [[7dd1]] – hChk Sprk1 + peptide
**[[3beg]] – hChk Srpk1 + splicing factor SF2
**[[3hdm]], [[3hdn]], [[7pue]] – hChk Sgk1 (mutant) + inhibitor
**[[2r5t]] – hChk Sgk3 + AMPPNP
**[[4yff]], [[4yfi]], [[6b5j]], [[7mgj]], [[7mgk]] – hChk Tnni3k + inhibitor
**[[2v3s]] – hChk Osr1 + hChk Wnk4 peptide
**[[2vwi]] – hChk Osr1 kinase domain + ANP
**[[7que]], [[7quf]] – hChk Drak1 kinase domain + inhibitor
**[[4crs]] – hChk N2 kinase domain + ATPγS
**[[3qfv]], [[3tku]], [[4ual]], [[5ote]], [[5otf]] – hChk Mrckβ + inhibitor
**[[4uak]] – hChk Mrckβ + ADP
**[[4cc9]], [[4z8l]], [[5aja]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
**[[5jk7]] – hChk Vprbp WD repeat domain + VPX + DDB1 + UDG
**[[3wa0]], [[4p7i]] – hChk Vprbp residues 1417-1506 + merlin
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[5ci7]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[5b5w]], [[5b6b]], [[5brk]] – hChk Lats1 residues 622-704 + MOB1
**[[5yz0]] – hChk Atr + Atr-interacting protein – Cryo EM
**[[6bdn]] – hChk Tao3 kinase domain + ADP
**[[5yh3]] – hChk Fam20C 141-578 + pseudokinase Fam20A
**[[2gcd]] – rChk Tao2 kinase domain + staurosporine
**[[1u5r]] – rChk Tao2 kinase domain + ATP
**[[5yj9]], [[7mp9]] – rfbChk Pink1 kinase domain + AMPPNP
**[[6bn1]] – DmChk Hippo SARAH domain + Shar-Pei
**[[3hgk]] – Chk Pto + effector protein AVRPTOB – Currant tomato
**[[3p86]], [[3ppz]] - AtChk Ctr1 + staurosporine
**[[4f0f]] – smChk Roco4 kinase domain + APPCP
**[[4f1m]], [[4f1o]] – smChk Roco4 kinase domain (mutant) + APPCP
**[[4f1t]], [[4yzm]], [[4yzn]] – smChk Roco4 kinase domain + inhibitor
**[[5fvm]] - Tor2 + LST8 - ''Kluyveromyces marxianus''
**[[5kc2]] - yVps15 + Vps34 - Cryo EM
**[[5dfz]] - yVps15 + Vps34 + Vps30 + VPSAP28 + VPSAP30 - Cryo EM
**[[1q8y]], [[1q97]], [[1q99]], [[1zyd]] – yChk + nucleotide
**[[1zy5]] – yChk (mutant) + nucleotide
**[[2jd5]] – yChk + NPL-3P
**[[4lqs]], [[4lqq]], [[4lqp]] – yChk Cbk1 residues 251-756 + Cbk1 activator Mob2
**[[6emk]] – yChk Tor2 + LST8 + TSC11 + AVO1 + AVO2 – Cryo EM
**[[6s8f]] – yChk Tel1 + AMPPNP – Cryo EM
**[[5yyz]] – yChk Mek1 FHA domain + Hop1
**[[5x6o]], [[6z3a]], [[7wzr]], [[7wzw]]– yChk Mec1 + LCD1 – Cryo EM
**[[6z2w]], [[6z2x]] – yChk Mec1 (mutant) + LCD1 – Cryo EM
**[[7kue]] – yChk Kin28 in TFIIK complex – Cryo EM
**[[6u6a]] – CaChk Yck2 + inhibitor
**[[5fvm]] – Chk Tor2 + LST8 – ''Kluyveromyces maximanus''
*Serine/threonine protein kinase Rad53 see [[Rad53]]
*Serine/threonine protein kinase Gsk3B see [[Glycogen synthase kinase 3]]
}}
[[Category:Topic Page]]

Serine/threonine protein kinase 3D structures

2026-08-19T07:44:03Z

Michal Harel:

==3D structures of serine/threonine protein kinase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Chk1'''; domains - kinase 1-289; KA1 393-492
**[[1ia8]] – hChk1 kinase domain – human
**[[5w12]] – hChk1 KA1 domain
**[[1zlt]] – hChk1 kinase domain + hymenaldisine
**[[1nvq]], [[1nvr]] – hChk1 kinase domain + peptide + saurosporine
**[[1nvs]], [[1zys]], [[7ako]] - hChk1 kinase domain + peptide + inhibitor
**[[7akm]] - hChk1 kinase domain + ATP
**[[2ayp]], [[2br1]], [[2brb]], [[2brg]], [[2brh]], [[2brm]], [[2brn]], [[2bro]], [[2c3j]], [[2c3k]], [[2c3l]], [[2cgu]], [[2cgv]], [[2cgw]], [[2cgx]], [[2e9n]], [[2e9o]], [[2e9p]], [[2e9u]], [[2e9v]], [[2gdo]], [[2ghg]], [[2hog]], [[2hxl]], [[2hxq]], [[2hy0]], [[2qhm]], [[2qhn]], [[2r0u]], [[3f9n]], [[2wmq]], [[2wmr]], [[2wms]], [[2wmt]], [[2wmu]], [[2wmv]], [[2wmw]], [[2wmx]], [[2xey]], [[2xf0]], [[2xez]], [[2x8d]], [[2x8e]], [[2x8i]], [[2ydi]], [[2ydj]], [[2ydk]], [[2yer]], [[2yex]], [[2ym3]], [[2ym4]], [[2ym5]], [[2ym6]], [[2ym7]], [[2ym8]], [[2ywp]], [[3jvr]], [[3jvs]], [[3nlb]], [[3ot3]], [[3ot8]], [[3pa3]], [[3pa4]], [[3pa5]], [[3tkh]], [[3tki]], [[3u9n]], [[4fsm]], [[4fsn]], [[4fsq]], [[4fsr]], [[4fst]], [[4fsu]], [[4fsw]], [[4fsy]], [[4fsz]], [[4ft0]], [[4ft3]], [[4ft5]], [[4ft7]], [[4ft9]], [[4fta]], [[4ftc]], [[4fti]], [[4ftj]], [[4ftk]], [[4ftl]], [[4ftm]], [[4ftn]], [[4fto]], [[4ftq]], [[4ftr]], [[4ftt]], [[4ftu]], [[4gh2]], [[4hyh]], [[4hyi]], [[4jik]], [[4qye]], [[4qyf]], [[4qyg]], [[4qyh]], [[4rvk]], [[4rvl]], [[4rvm]], [[5dls]], [[5f4n]], [[5fcf]], [[5fck]], [[6fc8]], [[6fcf]], [[6fck]], [[7bko]], [[8e80]], [[8e81]] - hChk1 kinase domain + inhibitor 
**[[5oot]], [[5op2]], [[5op4]], [[5op5]], [[5op7]], [[5opb]], [[5opr]], [[5ops]], [[5opu]], [[5opv]], [[5oq5]], [[5oq6]], [[5oq7]], [[5oq8]], [[7bjd]], [[7bjh]], [[7bjj]], [[7bjm]], [[7bjo]], [[7bjr]], [[7bjx]], [[7bk1]], [[7bk2]], [[7bk3]], [[7mck]], [[7suf]], [[7sug]], [[7suh]], [[7sui]], [[7suj]], [[8siv]], [[8siw]], [[8six]] - hChk1 kinase domain (mutant) + inhibitor
**[[5oop]] - hChk1 kinase domain (mutant) + AMPPNP
**[[5oor]] - hChk1 kinase domain (mutant) + staurosporine
**[[7bkn]] - hChk1 kinase domain + adenine
**[[7bje]] - hChk1 kinase domain (mutant) + adenine
**[[2jqi]] – yChk1 – yeast
*'''Chk2 (Checkpoint kinase)'''
**[[1gxc]] – hChk2 phosphothreonine-binding domain + phosphopeptide
**[[2cn5]] – hChk2 kinase domain + ADP
**[[2cn8]] – hChk2 kinase domain + inhibitor
**[[2cn8]], [[2uv2]], [[2w0j]], [[2w7x]], [[2wtc]], [[2wtd]], [[2wti]], [[2wtj]], [[2xbj]], [[2xk9]], [[2xm8]], [[2xm9]], [[2ycf]], [[2ycq]], [[2ycr]], [[2ycs]], [[2yiq]], [[2yir]], [[2yit]], [[4a9r]], [[4a9s]], [[4a9t]], [[4bda]], [[4bdb]], [[4bdc]], [[4bdd]], [[4bde]], [[4bdf]], [[4bdg]], [[4bdh]], [[4bdi]], [[4bdj]], [[4bdk]] - hChk2 kinase domain + inhibitor
**[[3i6u]], [[3i6w]] – hChk2 residues 84-502 (mutant)
*'''Chk3 (Mst2)'''; domains - kinase 13-313; SARAH 436-484
**[[3wws]], [[4hkd]], [[4l0n]], [[4oh9]] – hChk3 SARAH domain 
**[[4lg4]] – hChk3 kinase domain
**[[4lgd]] – hChk3 kinase domain + RASSF5 SARAH domain
**[[6ao5]] – hChk3 kinase+SARAH domains (mutant) + SAV1 SARAH domain
**[[5dh3]], [[8a66]] – hChk3 kinase domain + inhibitor
*'''Chk4 (Mst1)''' ; Domains – kinase 1-311; SARAH 432-480
**[[3com]] – hChk4 kinase domain
**[[6yat]], [[8a5j]]– hChk4 kinase domain + inhibitor
**[[4nr2]] – hChk4 SARAH domain
**[[2jo8]] – hChk4 SARAH domain - NMR
**[[4oh8]] – hChk4 SARAH domain + Ras association domain-containing protein
*'''Chk5 (Aurora kinase b)'''
**[[4af3]] – hChk5 + inhibitor
*'''Chk6 or Chk15 or Aurora kinase A'''
**[[1mq4]], [[1muo]], [[4j8n]], [[4o0s]], [[6cpe]] – hChk6 kinase domain 
**[[4bn1]], [[4o0w]], [[4o0u]] – hChk6 kinase domain (mutant)
**[[5dnr]], [[5drd]], [[5dt3]] – hChk6 kinase domain + ATP
**[[5drd]] – hChk6 kinase domain + ATP
**[[1ol6]] – hChk6 kinase domain (mutant) + ATP
**[[2wqe]] – hChk6 kinase domain (mutant) + ADP
**[[5odt]] – hChk6 kinase domain (mutant) + ADP + TACC3
**[[2c6d]] – hChk6 kinase domain (mutant) + ADPNP
**[[2dwb]] – hChk6 kinase domain + AMPPNP
**[[6cpf]] – hChk6 kinase domain + AMPPCP
**[[5g15]] – hChk6 kinase domain + AMPPNP + monobody
**[[6cpg]], [[8ssp]] – hChk6 kinase domain + inhibitor + monobody
**[[2j4z]], [[2j50]], [[2np8]], [[2x81]], [[2x6d]], [[2x6e]], [[3efw]], [[3myg]], [[3vap]], [[3w10]], [[3w16]], [[3w18]], [[3w2c]], [[4b0g]], [[4byi]], [[4byj]], [[4j8m]], [[4jai]], [[4jaj]], [[4uyn]], [[4uzd]], [[4uzh]], [[4zs0]], [[4ztq]], [[4ztr]], [[4zts]], [[5aad]], [[5aae]], [[5aag]], [[5dpv]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5obr]], [[5one]], [[5zan]], [[6c2r]], [[6c2t]], [[6gra]], [[6z4y]], [[7ayh]], [[7ayi]], [[7fic]], [[7o2v]], [[8jmx]] – hChk6 kinase domain + inhibitor 
**[[2bmc]], [[2c6e]], [[2wtw]], [[2xne]], [[2xng]], [[2xru]], [[3coh]], [[3fdn]], [[3h0y]], [[3h0z]], [[3h10]], [[3lau]], [[3k5u]], [[3m11]], [[3nrm]], [[3p9j]], [[3r21]], [[3r22]], [[3qbn]], [[3unz]], [[3uo4]], [[3uo5]], [[3uo6]], [[3uod]], [[3uoh]], [[3uoj]], [[3uok]], [[3uol]], [[3up2]], [[3up7]], [[4dea]], [[4deb]], [[4ded]], [[4dee]], [[4dhf]], [[4jbo]], [[4jbp]], [[4jbq]], [[4prj]], [[5aad]], [[5aae]], [[5aaf]], [[5aag]], [[5dpv]], [[6hjj]], [[6hjk]] – hChk6 kinase domain (mutant) + inhibitor 
**[[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[5dos]], [[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5dn3]], [[5dos]], [[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[6c83]] – hChk6 kinase domain + AMPPCP + nanobody
**[[8sso]] – hChk6 kinase domain + drug + monobody
**[[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5g1x]], [[7ztl]] – hChk6 kinase domain (mutant) + N-Myc
**[[8guw]] – hChk6 kinase domain/activator peptide
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + Targeting protein for XKLP2
**[[3d14]], [[3d15]], [[3d2i]], [[3d2k]] [[3daj]], [[3dj5]], [[3dj6]], [[3dj7]] – Chk6 kinase domain (mutant) + inhibitor - mouse 
*Chk6 with phosphorylated Thr 287, Thr288
**[[1ol5]], [[1ol7]] – hChk6 kinase domain + PThr + ADP
**[[5dnr]], [[5dt3]] – hChk6 kinase domain + PThr + ATP
**[[2w1c]], [[2w1d]], [[2w1e]], [[2w1f]], [[2w1g]], [[5dn3]] – hChk6 kinase domain + PThr + inhibitor
**[[2wtv]], [[5orl]], [[5orn]], [[5oro]], [[5orp]], [[5orr]], [[5ors]], [[5ort]], [[5orv]], [[5orw]], [[5orx]], [[5ory]], [[5orz]], [[5os0]], [[5os1]], [[5os2]], [[5os3]], [[5os4]], [[5os5]], [[5os6]], [[5osd]], [[5ose]], [[5osf]] – hChk6 kinase domain (mutant) + PThr + inhibitor
**[[3e5a]], [[3ha6]] – hChk6 kinase domain + PThr + inhibitor + targeting protein for XKLP2
**[[5g1x]] – hChk6 kinase domain (mutant) + PThr + N-Myc
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + PThr + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + PThr + TPX2
**[[6r4a]], [[6r4b]], [[6r4c]], [[6r4d]] – hChk6 kinase domain + PThr + inhibitor + ADP
**[[6i2u]] – hChk6 kinase domain (mutant) + PThr + inhibitor + ADP
**[[6r49]] – hChk6 kinase domain (mutant) + PThr + CoA
*'''Chk10 (lymphocyte-oriented kinase)''' or LOK or STK10
**[[7qgp]] – hChk10
**[[2j7t]], [[4aot]], [[4equ]], [[4usd]], [[4use]], [[5ajq]], [[5owq]], [[5owr]], [[6eim]], [[6gtt]], [[6hxf]], [[6i2y]] – hChk10 kinase domain + inhibitor
**[[4bc6]], [[6i2y]] – hChk10 + drug
*'''Chk11'''
**[[2wtk]] – hChk11 (mutant) + calcium-binding protein
*'''Chk12-A (Aurora kinase b-a or Aurora B kinase)'''
**[[2vgo]], [[2vgp]], [[2vrx]], [[3ztx]], [[4c2v]], [[5eyk]] – fChk12-A + inner centromere protein A peptide + inhibitor - frog
**[[4c2w]] – fChk12-A + inner centromere protein A peptide + AMPPNP
**[[4b8l]], [[4b8m]], [[5k3y]] – fChk12-A (mutant) + inner centromere protein A peptide + inhibitor
*'''Chk13 (Polo-like kinase Plk)'''
*Plk1 Polo-box domain (Pbd) 371-594''
**[[1q4o]], [[2ogq]], [[3hih]], [[3p2w]], [[4h5x]], [[6n46]] – hPlk1 Pbd
*Plk1 Pbd complex with polypeptide
**[[1umw]], [[2ojx]], [[3bzi]], [[3c5l]], [[3rq7]], [[4dfw]], [[4rcp]], [[4o6w]], [[4o56]], [[4whh]], [[4whk]], [[4whl]], [[5dms]], [[5dmv]], [[5dnj]] , [[7mso]], [[7mx1]] – hPlk1 + peptide
**[[3hik]], [[3fvh]], [[3p2z]], [[3p34]], [[3p35]], [[3p36]], [[3p37]], [[3q1i]], [[4e67]], [[4e9c]], [[4e9d]], [[4hab]], [[4hy2]], [[4o9w]], [[4x9r]], [[4x9v]], [[4x9w]], [[5j19]], [[6gy2]] – hPlk1 + phosphopeptide
**[[1q4k]] – hPlk1 (mutant) + phosphopeptide
**[[2v5q]] – hPlk1 + design ankyrin repeat protein
**[[4lkl]] – hChk Plk1 + PL-55
**[[4lkm]] – hChk Plk1 + PL-74
**[[6ax4]] – hChk Plk1 + histidine cyclized macrocycle
**[[5x3s]] – mPlk1 + phosphopeptide
**[[8joq]], [[8joy]] – hPlk1 Pbd + hpv peptide
*Plk1 Pbd complex with small molecule inhibitor
**[[4h71]], [[4hco]], [[5ta6]], [[5ta8]], [[8bjt]], [[8crc]] – hPlk1 + inhibitor
**[[2rku]] – hPlk1 (mutant) + inhibitor
**[[3db6]], [[3db8]], [[3dbc]], [[3dbd]], [[3dbe]], [[3dbf]] – zfPlk1 (mutant) + inhibitor – zebra fish
*Plk1 catalytic domain 36-345
**[[2owb]] – hPlk1 catalytic domain (mutant)
**[[2ou7]] – hPlk1 catalytic domain (mutant) + AM
**[[2yac]], [[3kb7]], [[3thb]], [[4a4l]], [[4a4o]] – hPlk1 catalytic domain + inhibitor
**[[3fc2]] – hPlk1 catalytic domain (mutant) + inhibitor
**[[4j52]], [[4j53]] – hChk Plk1 (mutant) + inhibitor
**[[3d5x]] – zfPlk1 catalytic domain (mutant) + wortmannin
**[[3d5w]] – zfPlk1 catalytic domain + ADP
*'''Plk2'''
**[[4i5m]], [[4i5p]], [[4i6b]], [[4i6f]], [[4i6h]] – hChk Plk2 kinase domain (mutant) + inhibitor
**[[4rs6]], [[4xb0]] – hChk Plk2 Pbd
*'''Plk3'''
**[[4b6l]], [[4i6b]] – hChk Plk3 kinase domain + inhibitor
*'''Plk4'''; Domains – kinase 2-275; Pbd 580-808; Pb3 884-970
**[[3cok]] – hChk Plk4 kinase domain
**[[4n9j]] – hChk Plk4 Pbd domain
**[[4n7v]], [[4n7z]] – hChk Plk4 Pbd domain + centrosomal protein
**[[6w38]], [[6w3i]] – hChk Plk4 Pbd domain + Fam46C
**[[6w3j]] – hChk Plk4 Pbd domain + Fam46C + CEP92 peptide
**[[4jxf]], [[4yur]] – hChk Plk4 kinase domain + inhibitor
**[[5lhy]] – hChk Plk4 Pb3 domain
**[[4yyp]], [[5lhz]] – hChk Plk4 Pb3 domain + Scl-interrupting locus protein
**[[4g7n]], [[4nk7]], [[5lhx]], [[7rl3]] – DmChk Plk4 Pbd domain – ''Drosophila melanogaster''
*'''Chk16'''
**[[2buj]] – hChk16 (mutant) + staurosporin
*'''Chk17B''' or DRAK2 or STK17B
**[[3lm0]] – hChk17B
**[[6qf4]], [[7q7c]], [[7q7d]] – hChk17B + ADP
**[[7q7e]] – hChk17B + ATP
**[[3lm5]] – hChk17B + quercetin
**[[6y6f]], [[6y6h]], [[6zjf]] – hChk17B + pyrimidine derivative
**[[7akg]] – hChk17B + drug
*'''Chk19''' or STK19
**[[7xrb]] – hChk19
*'''Chk24 (Mst3)''' or STK24
**[[3a7f]], [[3a7g]], [[3a7h]], [[3a7i]], [[3a7j]], [[3ckw]] – hChk24 kinase domain
**[[4qmm]], [[4qmn]], [[4qmo]], [[4qmp]], [[4qmq]], [[4qms]], [[4qmt]], [[4qmu]], [[4qmv]], [[4qmw]], [[4qmx]], [[4qmy]], [[4qmz]], [[4qna]], [[4qo9]], [[4u8z]], [[4w8d]], [[4w8e]], [[7b30]], [[7b31]], [[7b32]], [[7b33]], [[7b34]], [[7b35]], [[8bzi]], [[8bzj]], [[8qlr]], [[8qls]], [[8qlt]] – hChk Mst3 + inhibitor
**[[8qlq]] – hChk Mst3 + macrocyclic inhibitor
**[[3ckx]] – hChk24 kinase domain + staurosporin
**[[3zhp]] – hChk24 kinase domain + calcium-binding protein
**[[4o27]] – hChk24 kinase domain (mutant) + calcium-binding protein
**[[4qml]] – hChk Mst3 kinase domain + AMPPNP
*'''Chk25 or STK25'''
**[[2xik]] – hChk25 kinase domain
**[[7z4v]] – hChk25 kinase domain + inhibitor
**[[3w8h]] – hChk25 regulatory domain + programmed cell death protein 10
**[[4nzw]] – hChk25 kinase domain (mutant) + calcium-binding protein
*'''Chk26 (Mst4)'''
**[[3ggf]], [[7b36]] – hChk Mst4 + inhibitor
**[[[3w8i]], [4geh]] - hChk Mst4 dimerization domain + programmed cell death protein 10
**[[4fza]], [[4fzd]], [[4fzf]] – hChk Mst4 (mutant) + calcium-binding protein
*'''Chk32'''
**[[4fr4]] – hChk32A
*'''Chk38'''
**[[6bxi]] – hChk38 kinase domain
*'''Chk39''' or SPAK
**[[7o86]] – hChk39 C-terminal
**[[5d9h]] – mChk39 residues 63-403 + ATP
**[[5dbx]] – mChk39 residues 63-403 (mutant) + AMPPNP
*'''Chk40'''
**[[5l2q]] – hChk40 kinase homology domain
*'''Dclk1'''
**[[6kyq]] – hChk Dclk1 kinase domain
**[[6kyr]] – hChk Dclk1 kinase domain (mutant)
**[[5jzj]] – hChk Dclk1 kinase domain + AMPPN
**[[5jzn]], [[7kx6]], [[7kxw]] – hChk Dclk1 kinase domain + inhibitor
**[[7f3g]] – hChk Dclk1 kinase domain + drug
**[[7kx8]] – hChk Dclk1 C-terminal + inhibitor
*'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123; kinase 144-480
**[[1unp]], [[1unr]] – hRac-α hChk pleckstrin homology domain
**[[2uzr]], [[2uzs]], [[7myx]] – hRac-α hChk pleckstrin homology domain (mutant)
**[[1h10]], [[1unq]], [[2uvm]] – hRac-α hChk pleckstrin homology domain + inositol tetrakisphosphate
**[[3o96]], [[4ejn]], [[6hhf]], [[6hhg]], [[6hhh]], [[6hhi]], [[6hhj]], [[6s9w]], [[6s9x]] - hRac-α hChk + inhibitor
**[[5kcv]], [[7nh4]], [[7nh5]] - hRac-α hChk (mutant) + inhibitor
**[[4ekl]], [[4gv1]] - hRac-α hChk kinase domain + inhibitor
**[[3qkm]], [[6ccy]] - hRac-α hChk kinase domain (mutant) + inhibitor
**[[6buu]] - hRac-α hChk kinase domain + bisubstrate peptide
**[[4ekk]] - hRac-α hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[6npz]] - hRac-α hChk kinase domain + peptide + inhibitor
**[[3ow4]], [[3qkk]], [[3qkl]], [[6buu]] - hRac-α hChk kinase domain (mutant) + peptide + inhibitor
**[[7apj]] - hRac-α hChk + nanobody
*'''Rac-β hChk (AKT2)'''
**[[1gzk]], [[1gzn]], [[1gzo]], [[1mrv]], [[1mry]] – hRac-β hChk kinase domain
**[[1p6s]] - hRac-β hChk pleckstrin homology domain - NMR
**[[1o6k]] - hRac-β hChk kinase domain + GSK3 peptide + AMPPNP
**[[2jdo]], [[2jdr]], [[2uw9]], [[2x39]], [[3cqu]], [[3cqw]] - hRac-β hChk kinase domain + GSK3 peptide + inhibitor
**[[3e87]], [[3e88]], [[3e8d]] - Rac-β hChk kinase domain (mutant) + GSK3 peptide + inhibitor<br /
**[[1o6l]] - hRac-β hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[3d0e]], [[8q61]] - hRac-β hChk kinase domain (mutant) + inhibitor
*'''Rac-γ hChk (ATK3)'''
**[[2x18]] – Rac-γ hChk PH domain
*'''A-Raf'''
**[[1wxm]] – hA-Raf RAS-binding domain 19-91 - NMR
**[[2mse]] – hA-Raf RAS-binding domain + APOA-I + K-ras - NMR
*'''B-Raf'''; domains - BRS 38-116; Ras-binding 153-237; kinase 445-723
**[[8dgs]], [[8dgt]] – hB-Raf in Ras/Raf complex – Cryo EM
**[[7z37]], [[7z38]], [[7zr5]] – hB-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
**[[1uwh]], [[3c4c]], [[6v2u]], [[6xfp]], [[6xlo]], [[8f7o]], [[8f7p]] – hB-Raf kinase domain + anticancer drug
**[[1uwj]], [[6p3d]] – hB-Raf kinase domain (mutant) + anticancer drug
**[[2fb8]], [[3d4q]], [[3e26]], [[3ii5]], [[3ppj]], [[3ppk]], [[3prf]], [[3pri]], [[3psb]], [[3psd]], [[3q4c]], [[3q96]], [[3skc]], [[3tv4]], [[3tv6]], [[4dbn]], [[4e26]], [[4e4x]], [[4ehe]], [[4fc0]], [[4g9c]], [[4h58]], [[4ksp]], [[4ksq]], [[4mbj]], [[4pp7]], [[6cad]], [[7shv]] – hB-Raf kinase domain + pyrazole inhibitor 
**[[3idp]], [[4ehg]], [[4fk3]], [[4g9r]], [[4jvg]], [[4mnf]], [[4r5y]], [[4rzv]], [[4rzw]], [[4wo5]], [[4xv1]], [[4xv2]], [[4xv3]], [[4xv9]], [[4yht]], [[5c9c]], [[5hi2]], [[5ita]], [[5jrq]], [[5jsm]], [[5jt2]], [[6nsq]], [[6p7d]], [[6uuo]] – hB-Raf kinase domain (mutant) + pyrazole inhibitor
**[[5csw]], [[5csx]], [[5ct7]], [[5fd2]], [[5hid]], [[5hie]], [[5val]], [[5vam]], [[6b8u]], [[6n0p]], [[6n0q]], [[7k0v]], [[7p3b]], [[7p3v]], [[8c7x]], [[8c7y]] - hB-Raf kinase domain + inhibitor
**[[6v34]] – hB-Raf kinase domain (mutant) + inhibitor
**[[4mne]] – hB-Raf kinase domain + MAPKK1
**[[8f7o]] – hB-Raf kinase domain + drug
**[[7m0u]] – hB-Raf kinase domain + AMPPNP + drug
**[[6u2h]] – hB-Raf kinase domain + 14-3-3 ζ/δ
**[[7mfe]] – hB-Raf + 14-3-3 ζ/δ – Cryo EM
**[[7mff]] – hB-Raf + 14-3-3 ζ/δ + inhibitor – Cryo EM
**[[7mfd]] – hB-Raf + 14-3-3 ζ/δ + MEK + inhibitor – Cryo EM
**[[6pp9]] – hB-Raf kinase domain + MEK1 + ANP
**[[7m0x]], [[7m0z]] – hB-Raf kinase domain + MEK1 + ANP + inhibitor
**[[7m0t]], [[7m0u]], [[7m0v]], [[7m0w]], [[7m0y]] – hB-Raf kinase domain + MEK1 + ANP + drug
**[[6u2g]] – hB-Raf kinase domain + MEK1 + AMPPCP
**[[5vr3]] – hB-Raf BRS domain
**[[7jhp]] – hB-Raf BRS domain + Hras
**[[6ntc]], [[6ntd]] – hB-Raf BRS domain (mutant) + Hras
**[[6xi7]] – hB-Raf 52-188 + Kras
**[[2l05]], [[5j17]], [[5j2r]] – hB-Raf RAS-binding domain - NMR
**[[3ny5]] – hB-Raf RAS-binding domain
**[[5j18]] – hB-Raf RAS-binding domain + inhibitor - NMR
**[[6pts]], [[6ptw]] – hB-Raf 56-187 + Kras + apolipoprotein + GMPPNP - NMR
**[[6q0k]], [[6uan]] – hB-Raf + 14-3-3 ζ – Cryo EM
**[[6nyb]] – hB-Raf + 14-3-3 ζ + MEK1 – Cryo EM
**[[6q0t]], [[6q0j]] – hB-Raf (mutant) + 14-3-3 ζ + MEK1 – Cryo EM
*'''c-Raf'''; Domains – RAS-binding (RBD) 55-132; Cys-rich 136-187 (CBD); kinase 323-618
**[[1rfa]], [[8jna]], [[8jof]], [[8jog]] – hc-Raf RBD - NMR
**[[1faq]], [[1far]] – hc-Raf cysteine-rich domain - NMR
**[[3omv]] – hc-Raf kinase domain
**[[1rrb]] – c-Raf RBD – NMR - rat
*c-Raf complex with protein
**[[8cpd]] – hc-Raf + 14-3-3 protein zeta – Cryo EM
**[[9mmp]] – hc-Raf + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[9mmr]] – hc-Raf (mutant) + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[1c1y]] – hc-Raf RBD + RAP1A
**[[3kuc]] – hc-Raf RBD (mutant) + RAP1A
**[[1gua]] – hc-Raf RBD + RAP1A + GPPNHP
**[[8jnb]] – hc-Raf RBD + ligand
**[[4g0n]], [[4g3x]] – hc-Raf RBD + GTPase Hras
**[[3kud]] – hc-Raf RBD (mutant) + GTPase Hras
**[[8epw]], [[8t74]] – hc-Raf RBD + GTPase K-ras
**[[8t75]], [[9ygs]] – hc-Raf RBD-CRD + GTPase K-ras + GMPPNP
**[[9ay7]], [[9aya]] – hc-Raf + MEK1
**[[9mmq]] – hc-Raf + MEK1 – Cryo EM
**[[9mms]] – hc-Raf (mutant) + MEK1 – Cryo EM
**[[9o0u]], [[9o0v]] – hc-Raf (mutant) + MEK1 + ANP + inhibitor– Cryo EM
**[[8u1l]] – hc-Raf + Hsp90 + CDC37 – Cryo EM
**[[8gae]], [[8gft]] – hc-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
*'''Snf1-related Chk'''
**[[3uc4]], [[3uc3]], [[3udb]], [[3zut]], [[3zuu]] – AtChk Srk2E kinase domain (mutant) – ''Arabidopsis thaliana''
**[[3ujg]] – AtChk Srk2E kinase domain (mutant) + protein phosphatase 2C
**[[5yks]] – hChk
*'''MAPK-interacting Chk''' or Mnk1 Mnk2
**[[2hw6]] – hMnk 1 catalytic domain
**[[2hw7]] – hMnk 1 catalytic domain + staurosporin
**[[5wvd]] – hMnk 1 catalytic domain + inhibitor
**[[2ac3]] – hMnk 2 catalytic domain
**[[2ac5]] – hMnk 2 catalytic domain (mutant)
**[[6cj5]], [[6cje]], [[6cjh]], [[6cjw]], [[6cjy]], [[6ck3]], [[6ck6]], [[6cki]] – hMnk 2 catalytic domain (mutant) + inhibitor
*'''hChk Pak''' or '''Chk N''' or '''PRK1'''; Domains - CRIB 74-109; Hr1B 122-199; catalytic 109-426; kinase 605-942
**[[1urf]] – hChk Pak-1 Hr1b domain - NMR
**[[4nkg]] – hChk Pak-1 Hr1b domain + SSPH1 LRR domain
**[[2rmk]] – hChk Pak-1 Hr1bb domain + Rac1 - NMR
**[[1f3m]] – hChk Pak-1 autoregulatory+kinase domains
**[[4otd]] - hChk Pak-1 kinase domain
**[[1yhv]], [[1yhw]], [[3q4z]], [[3q52]], [[3q53]] – hChk Pak-1 kinase domain (mutant)
**[[4o0r]], [[4o0t]], [[4zji]], [[4zjj]], [[4zlo]], [[4zy4]], [[4zy5]], [[4zy7]], [[5ime]], [[5kbq]], [[5kbr]], [[6b16]], [[7vto]] – hChk Pak-1 kinase domain + inhibitor
**[[4oti]], [[4oth]], [[4otg]] – hChk Pak-1 kinase domain + inhibitor
**[[4eqc]], [[4p90]], [[5dew]], [[5dey]], [[5dfp]] – hChk Pak-1 kinase domain (mutant) + inhibitor
**[[2hy8]] – hChk Pak-1 kinase domain + staurosporin
**[[2qme]] – hChk Pak-1 CRIB domain + RAC3
**[[3fxz]], [[3fy0]], [[4daw]] – hChk Pak-1 kinase domain (mutant) + Ru complex
**[[6fd3]] – hChk Pak-3 kinase domain (mutant)
**[[2j0i]], [[4fie]] – hChk Pak-4
**[[4fig]], [[4fij]], [[4l67]] – hChk Pak-4 kinase domain
**[[2cdz]] – hChk Pak-4 + purine derivative
**[[2ov2]] – hChk Pak-4 CRIB domain + RAC3
**[[2qon]], [[4fif]], [[4fih]], [[4fii]], [[4jdh]], [[4jdi]], [[4jdj]], [[4jdk]], [[6wlx]], [[6wly]] – hChk Pak-4 kinase domain + peptide
**[[4app]], [[4o0v]], [[4o0x]], [[4o0y]], [[4njd]], [[4xbu]], [[5bms]], [[5i0b]], [[5vee]], [[5vef]], [[5zjw]], [[5xvg]], [[5xvf]], [[5xva]], [[7cmb]], [[7cp3]], [[7cp4]] – hChk Pak-4 kinase domain + inhibitor
**[[2x4z]], [[2xh5]] – hChk Pak-4 kinase domain (mutant) + inhibitor
**[[5upl]], [[5upk]] – hChk Pak-4 kinase domain (mutant) + CDC42
**[[5ved]] – hChk Pak-4 kinase domain + staurosporine
**[[8ahi]] – hChk Pak-4 300-591 + inhibitor
**[[7s46]], [[7s48]] – hChk Pak-4 catalytic domain + integrin beta-5 peptide
**[[2c30]] – hChk Pak-6
**[[2odb]] – hChk Pak-6 CRIB domain + CDC42
**[[4ks8]] – hChk Pak-6 kinase domain + sunitinib
**[[4ks7]] – hChk Pak-6 kinase domain (mutant) + inhibitor
**[[2f57]] – hChk Pak-7
*'''Mycobacterium tuberculosis Chk Pkn'''
**[[4x3f]] - MtChk PknA – ''Mycobacterium tuberculosis''
**[[4ow8]] - MtChk PknA kinase domain
**[[3ori]], [[3ork]], [[3orl]], [[3orm]], [[3oro]], [[3orp]], [[3ort]] - MtChk PknB kinase domain (mutant)
**[[1o6y]] – MtChk PknB kinase domain
**[[6b2p]], [[6b2q]] – MtChk PknB kinase domain + inhibitor
**[[2kud]], [[2kue]], [[2kuf]], [[2kui]] – MtChk PknB pasta domains 2-3 - NMR
**[[3ouv]] – MtChk PknB pasta domain 3
**[[5e0y]] – MtChk PknB pasta domain 4
**[[5e10]] – MtChk PknB pasta domains 1-2
**[[5e0z]] – MtChk PknB pasta domains 3-4
**[[5e12]] – MtChk PknB pasta domains 2-4
**[[5u94]] - MtChk PknB kinase domain + inhibitor
**[[3f61]], [[3f69]] - MtChk PknB kinase domain (mutant) + inhibitor
**[[6i2p]] - MtChk PknB kinase domain (mutant) + GARA + peptide
**[[1rwi]], [[1rwl]] - MtChk PknD extracellular domain
**[[2h34]] – MtChk PknE catalytic domain
**[[7naa]] – MtChk PknF kinase domain + inhibitor
**[[4y12]] - MtChk PknG + ATP-gS
**[[4y0x]] - MtChk PknG + ADP
**[[7q52]] - MtChk PknG + inhibitor
**[[4esq]] - MtChk PknH extracellular domain
**[[5m06]], [[5xka]] - MtChk PknI kinase domain
**[[5m07]], [[5m08]], [[5m09]] - MtChk PknI kinase domain (mutant)
**[[5xlm]], [[5xll]] - MtChk PknI sensor domain
**[[7mxb]], [[7mxj]], [[7mxk]] - Chk PknG kinase domain + AMPPNP - Corynebacterium glutamicum
*'''hChk Nek'''
**[[4apc]] – hChk Nek1 kinase domain (mutant)
**[[4b9d]] - hChk Nek1 kinase domain (mutant) + inhibitor
**[[2w5h]] – hChk Nek2 kinase domain
**[[2jav]], [[2wqo]], [[2xk3]], [[2xk4]], [[2xk6]], [[2xk7]], [[2xk8]], [[2xkc]], [[2xkd]], [[2xke]], [[2xkf]], [[2xnm]], [[2xnn]], [[2xno]], [[2xnp]], [[4a4x]], [[4afe]], [[5m51]], [[5m53]], [[5m55]], [[5m57]], [[6sgd]], [[6sgh]], [[6sgi]], [[6sgk]], [[6sk9]] – hChk Nek2 + inhibitor
**[[2w5a]], [[2w5b]] – hChk Nek2 + nucleotide
**[[6tm5]] - hChk Nek2 in anaphase-promoting complex – Cryo EM
**[[2wqm]], [[6s76]] – hChk Nek7
**[[2wqn]] – hChk Nek7 + ADP
**[[5de2]] – hChk Nek7 + hChk Nek9
**[[6s73]], [[2wqo]] – hChk Nek7 + inhibitor
**[[6npy]] – hChk Nek7 + Nlrp3
**[[6s75]] – hChk Nek7 + inhibitor
*'''Chk Rio'''
**[[6fdo]], [[6fdn]], [[6fdm]] – hChk Rio2
**[[4otp]] – hChk Rio1 Rio domain + ADP
**[[6hk6]], [[7vbt]] – hChk Rio2 + inhibitor
**[[6eml]], [[6fai]], [[6g18]], [[6g51]], [[6rbd]],[[6rbe]], [[6y7c]] – yChk Rio2 in 40S particle – Cryo EM
**[[1ztf]] – AfChk Rio1 + adenine derivative – Archaeoglobus fulgidus
**[[1zth]] – AfChk Rio1 + ADP
**[[1zp9]] – AfChk Rio1 + ATP
**[[1tqp]], [[1zao]] – AfChk Rio2 + ATP
**[[1zar]] – AfChk Rio2 + ADP
**[[4gyg]] – CtChk Rio2 – Chaetonium thermophilum
**[[4gyi]] – CtChk Rio2 + ADP
*hChk Vrk (vaccinia-related kinase)
**[[2kty]], [[2kul]], [[2lav]], [[2rsv]] – hChk Vrk1 kinase domain 1-396 - NMR
**[[3op5]] – hChk Vrk1 kinase domain (mutant)
**[[5ukf]] – hChk Vrk1 kinase domain + inhibitor
**[[5uvf]], [[6cnx]], [[6bu6]], [[6cfm]], [[6dd4]], [[6bp0]], [[6bru]], [[6btw]], [[6cmm]], [[6cqh]], [[6csw]], [[6npn]], [[6vxu]], [[6vzh]] – hChk Vrk1 kinase domain (mutant) + inhibitor
**[[6ac9]] – hChk Vrk1 kinase domain (mutant) + AMPPNP
**[[7tan]] – hChk Vrk1 kinase domain + nucleosome – Cryo EM
**[[2v62]] – hChk Vrk2 kinase domain
**[[5uu1]], [[6ncg]], [[8q1z]] – hChk Vrk2 kinase domain + inhibitor
*Chk Wnk (protein kinase lysine-deficient); Domains - kinase 194-483; CCT1 454-549
**[[6cn9]], [[4q2a]], [[4pwn]] - hChk Wnk1 kinase domain (mutant)
**[[5tf9]] - hChk Wnk1 kinase domain + inhibitor + AMPPNP
**[[5wdy]], [[5we8]] - hChk Wnk1 kinase domain + inhibitor + ANP
**[[5drb]], [[6ol2]]- rChk Wnk1 kinase domain (mutant) + inhibitor
**[[6elm]] - hChk Wnk2 CCT1 domain
**[[6fbk]] - hChk Wnk2 CCT1 domain + Wnk1 peptide
**[[5o1v]], [[5o21]], [[5o23]] - hChk Wnk3 kinase domain
**[[5o2c]] - hChk Wnk3 kinase + CCT1 domains
**[[5o26]], [[5tf9]] - hChk Wnk3 kinase domain + AMPPNP
**[[5o2b]] - hChk Wnk3 kinase domain + inhibitor
**[[8edh]] - hChk Wnk3 kinase domain (mutant) + inhibitor
**[[2lru]] – rChk Wnk1 autoinhibitory domain 480-572 - NMR
**[[5w7t]] - rChk Wnk1 kinase domain
**[[7uos]] - rChk Wnk1 kinase domain (mutant)
*'''TANK-binding kinase'''
**[[4efo]] – hChk Tbk1 ubiquitin-like domain
**[[6rsr]], [[6rsu]] – hChk Tbk1 + inhibitor
**[[4im0]], [[4im2]], [[4im3]], [[4iw0]], [[4iwo]], [[4iwp]], [[4ipq]], [[6rst]] – hChk Tbk1 (mutant) + inhibitor
**[[6cq5]], [[6cq4]], [[6cq0]], [[6boe]], [[6bod]], [[6bny]], [[5w5v]] – hChk Tbk1 + ulcer drug
**[[4eut]], [[4euu]] – hChk Tbk1 kinase+ubiquitin-like domains (mutant) + inhibitor
**[[6nt9]] – hChk Tbk1 (mutant) + STING
**[[5eoa]], [[5eof]] – hChk Tbk1 residues 677-729 + optineurin
**[[4jl9]], [[4jlc]] – mChk Tbk1 + inhibitor
**[[6o8c]], [[6o8b]] – mChk Tbk1 (mutant) + STING
*'''Haspin'''
**[[2vuw]], [[2wb8]] – hChk Haspin kinase domain
**[[3dle]] – hChk Haspin kinase domain + AMP
**[[3e7v]], [[3f2n]], [[3fmd]], [[3iq7]], [[4qtc]], [[5htb]], [[5htc]], [[6z56]], [[6z57]], [[6z58]], [[6z59]], [[6z5a]], [[6z5b]], [[6z5c]]. [[6z5d]], [[6z5e]] , [[7avq]], [[7ops]] – hChk Haspin kinase domain + inhibitor
**[[7sqm]] – hChk Haspin kinase domain + antimalarial
**[[6g38]], [[6g34]], [[6g35]], [[6g36]], [[6g37]] – hChk Haspin kinase domain + tubercidin derivative
**[[6g39]], [[6g3a]] – hChk Haspin kinase domain (mutant) + tubercidin derivative
**[[4ouc]] – hChk Haspin kinase domain + histone H3 peptide
*'''MAP/microtubule affinity-regulating kinase (MARK)'''
**[[2hak]] – hChk MARK1 catalytic+UBA domains
**[[3ose]] - hChk MARK1 KA1 domain
**[[6c9d]] – hChk MARK1 catalytic+UBA+KA1 domains (mutant)
**[[5eak]], [[5kz7]], [[5kz8]] – hChk MARK2 catalytic+UBA domains + inhibitor
**[[3iec]] – hChk MARK2 catalytic+UBA domains + cytotoxicity-associated immunodominant antigen peptide
**[[2qnj]] – hChk MARK3 catalytic+UBA domains
**[[3fe3]] – hChk MARK3 catalytic+UBA domains (mutant)
**[[7p1l]] – hChk MARK3 catalytic+UBA domains + inhibitor
**[[5es1]] – hChk MARK4 catalytic+UBA domains + inhibitor
**[[1zmu]] – rChk MARK2 catalytic+UBA domains
**[[2wzj]], [[2r0i]], [[1zmv]], [[1y8g]], [[1zmw]] – rChk MARK2 catalytic+UBA domains (mutant)
**[[1ul7]], [[1v5s]] - mChk MARK3 catalytic domain - NMR
*'''Mitotic checkpoint Chk (Bub)'''; Domains: TPR 1-220; kinase 726-1085
**[[2lah]] – hChk Bub1 TPR domain – NMR
**[[2wvi]] – hChk Bub1β TPR domain
**[[3si5]] – hChk Bub1 TPR domain + CASC5 peptide
**[[4r8q]], [[4qpm]], [[5dmz]] – hChk Bub1 kinase domain + ADP
**[[6f7b]] – hChk Bub1 kinase domain + inhibitor
**[[4a1g]] – hChk Bub1 TPR domain + CASC5 KI motif
**[[4ggd]] - hChk Bub1 + cell division cycle protein
**[[6tlj]], [[5khu]] - hChk Bub1 in anaphase-promoting complex – Cryo EM
**[[6jkk]] – DmChk Bub1 kinase domain
**[[6jkm]] – DmChk Bub1 kinase domain + ADP
**[[5jja]] – hChk Bub1 residues 661-734 + PP2A
**[[3esl]] – yChk Bub1 N terminal
**[[4bl0]] - yChk Bub1 + cell cycle arrest protein Bub3
*'''Microtubule-associated Chk'''
**[[2m9x]] – hChk 1 residues 187-287 – NMR
**[[3ps4]] - hChk 1 residues 965-1057
**[[2kqf]], [[2kyl]] – hChk 2 PDZ domain + glycoprotein C terminal – NMR
**[[3khf]] - hChk 3 PDZ domain
**[[2w7r]] – hChk 4 PDZ domain
*'''mTOR''' or '''Mechanistic target of rapamycin'''
*''mTOR FRB domain residues 2015-2114''
**[[1nsg]], [[1fap]] – hFRAP FRB domain + FKBP
**[[2rse]] – hFRAP FRB domain + FKBP – NMR
**[[1aue]] – hFRAP FRB domain
**[[2gaq]], [[2npu]] – hFRAP FRB domain - NMR
**[[8ppz]] – hFRAP FRB domain + FKBP + pyridine derivative
**[[3fap]], [[2fap]], [[4fap]] – hFRAP FRB domain + FKBP + rapamycin analog
**[[4drh]], [[4dri]], [[4drj]], [[5gpg]] – hFRAP FRB domain + FKBP + rapamycin
**[[6m4u]], [[6m4w]] – hChk Mtor FRB domain (mutant) + FKBP1A + rapamycin
**[[5wbh]] – hFRAP FRB domain + S6K1 peptide
*''mTOR FAT+PIKK domain residues 1376-2549''
**[[4jsn]] – hFRAP + TORC subunit LST8
**[[4jsp]] – hFRAP + TORC subunit LST8 + ATP
**[[4jsv]] – hFRAP + TORC subunit LST8 + ADP
**[[4jsx]] – hFRAP + TORC subunit LST8 + torin2
**[[4jt5]] – hFRAP + TORC subunit LST8 + pp242
**[[4jt6]] – hFRAP + TORC subunit LST8 + PI-103
**[[5wby]], [[5wbu]] – hFRAP + TORC subunit LST8 + proline-rich Akt1 substrate
*''mTOR complex''
**[[5flc]] – hmTOR + RAPTOR + LST8 + FKBP – Cryo EM
**[[5h64]] – hmTOR + RAPTOR + LST8 – Cryo EM
**[[6sb2]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC – Cryo EM
**[[6sb0]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC + proline-rich Akt1 substrate – Cryo EM
**[[5zcs]] – hmTOR + LST8 + AVO3 + TORC2 – Cryo EM
**[[7tzo]] – hTORC2 in mTORC2 complex– Cryo EM
**[[6zwm]], [[6zwo]], [[7owg]], [[7pe7]], [[7pe8]], [[7pe9]], [[7pea]], [[7peb]], [[7pec]], [[7uxc]] , [[8era]]– mTOR in mTor complex – Cryo EM
*'''Gcn2'''
**[[1zyc]] – yChk Gcn2
**[[1zxe]], [[1zy4]], [[1zy5]] – yChk Gcn2 (mutant)
**[[2yz0]] – yChk Gcn2 RWD/GI domain – NMR
**[[4otm]] – yChk Gcn2 C terminal domain
**[[1zyd]] – yChk Gcn2 + ATP
**[[4otn]] – mChk Gcn2 C terminal domain
*'''LRRK1''' or leucine-rich repeat Chk1
**[[8e04]], [[8e05]], [[8e06]], [[8fac]] – hLRRK1 – Cryo EM
*'''LRRK2''' or leucine-rich repeat Chk2 or dardarin
**[[6xr4]] – hLRRK2 – Cryo EM
**[[7lht]], [[7lhw]], [[7li4]] – hLRRK2 + ATP + GDP – Cryo EM
**[[7li3]] – hLRRK2 (mutant) + ATP + GDP – Cryo EM
**[[6oje]], [[7thy]] – hLRRK2 GTPase domain 1329-1520
**[[6ojf]] – hLRRK2 GTPase domain (mutant)
**[[6dlo]], [[6dlp]] – hLRRK2 WD40 domain
**[[7thz]] – hLRRK2 1330-1527 + GDP
**[[6vno]], [[6vp6]], [[6vp7]] – hLRRK2 C terminal 1330-2527 – Cryo EM
**[[6vp8]] – hLRRK2 C terminal 1330-2527 + COR domain 1670-1950 + WD40 domain 2140-2489 – Cryo EM
**[[6s6q]] – AtLRRK2 ectodomain + protein casparian strip peptide
*'''Pim'''
*Pim1 catalytic domain residues 14-313
**[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain
**[[1yxs]] – hPim1 catalytic domain (mutant)
**[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP
**[[1yxu]] – hPim1 catalytic domain + AMP
**[[1yxv]], [[5ipj]] – hPim1 catalytic domain + quinoline derivative
**[[1yxx]] – hPim1 catalytic domain + indole derivative
**[[2bzh]], [[2bzi]], [[2bzj]] – hPim1 catalytic domain (mutant) + organometallic ligand
**[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3c4e]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umw]], [[3umx]], [[4enx]], [[4eny]], [[4k1b]], [[4k18]], [[4k0y]], [[4iaa]], [[4i41]], [[4ll5]], [[4lm5]], [[4lmu]], [[4mta]], [[4med]], [[4mbl]], [[4mbi]], [[4n6y]], [[4n6z]], [[4n70]], [[4xh6]], [[5iis]], [[5kgd]], [[5kge]], [[5kgg]], [[5kgi]], [[5kgk]], [[5kzi]], [[5vua]], [[5vub]], [[5vuc]], [[6mt0]], [[6vrv]], [[7oov]], [[7oow]], [[7oox]], [[7xsv]] – hPim1 catalytic domain + inhibitor
**[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor
*Pim1 kinase domain residues 92-404
**[[4jx3]] – hPim1 kinase domain
**[[3uix]], [[5c1q]] – hPim1 kinase domain residues 120-404 + quinoline derivative
**[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate
**[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand
**[[1xws]], [[4alu]], [[4alv]], [[4alw]], [[4as0]], [[4bzn]], [[4bzo]], [[4dtk]], [[4jx7]], [[4rbl]], [[4rc2]], [[4rc3]], [[4rc4]], [[4ty1]], [[4wrs]], [[4wsy]], [[4wt6]], [[4xhk]], [[5dgz]], [[5dhj]], [[5dia]], [[5dwr]], [[5eol]], [[5kcx]], [[5o11]], [[5o12]], [[5o13]], [[5tel]], [[5tex]], [[5toe]], [[5v80]], [[5v82]]. [[6bsk]], [[6kzi]], [[6l11]], [[6l12]], [[6l13]], [[6l14]], [[6l15]], [[6l16]], [[6l17]], [[6no8]], [[6no9]], [[6vru]], [[6ykd]], [[7zun]] – hPim1 kinase domain + inhibitor
**[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor
*Pim1 full length
**[[4rpv]], [[5tur]] - hPim1 + inhibitor
*Pim1 complex with consensus peptide (pimtide)
**[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6qxk]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]] – hPim1 kinase domain + inhibitor + consensus peptide
**[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide
**[[2c3i]], [[5ndt]], [[5n5m]], [[5n5l]], [[5n52]], [[5n51]], [[5n50]], [[5n4z]], [[5n4y]], [[5n4x]], [[5n4v]], [[5n4u]], [[5n4r]], [[5n4o]], [[5n4n]], [[5mzl]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide
**[[4gw8]], [[7qb2]], [[7qfm]], [[7z6u]], [[8afr]] – hPim1 catalytic domain (mutant) + inhibitor + pimtide
**[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide
**[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide
*Pim1 containing phosphorylated Ser 261
**[[1yhs]] – hPim1 kinase domain + PSer + staurosporine
**[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor
**[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor
**[[1yi4]] – hPim1 kinase domain + PSer + adenosine
*Pim2
**[[4x7q]] – hPim2 catalytic domain + inhibitor
**[[2iwi]] – hPim2 catalytic domain + Ru ligand
*'''Rip or receptor-interacting Chk; Domains – catalytic 1-294; Amyloid fibril 418-518; Death 561-671'''
**[[6ac5]] – hRip1 death domain
**[[6r5f]], [[6nw2]], [[6c4d]], [[6c3e]], [[5tx5]], [[7fcz]], [[7fd0]], [[7ydx]] – hRip1 catalytic domain + inhibitor
**[[6rln]], [[6ocq]], [[6nyh]], [[6hho]] – hRip1 catalytic domain (mutant) + inhibitor
**[[6ggs]] – hRip2 – Cryo EM
**[[5yrn]] – hRip2 CARD domain 434-540 – Cryo EM
**[[6szj]], [[6sze]], [[6s1f]], [[6rna]], [[6rn8]], [[6hmx]], [[6fu5]], [[6es0]], [[5w5o]], [[5w5j]] – hRip2 catalytic domain + inhibitor
**[[6ul8]] – hRip2 catalytic domain (mutant) + inhibitor
**[[8aza]] – hRip2 catalytic domain + XiaP Bir2 domain – Cryo EM
**[[7mx3]] – hRip3 catalytic domain (mutant) + inhibitor
**[[7mon]] – hRip3 catalytic domain (mutant) + MLKL
**[[7dac]] – hRip3 amyloid fibril - NMR
**[[7da4]] – hRip3 amyloid fibril – Cryo EM
**[[6oko]] – mRip3 catalytic domain + inhibitor
**[[6jpd]] – mRip3 residues 409-486 - NMR
**[[5wnm]], [[5wnj]] – mRip4 catalytic domain (mutant) + drug
**[[5wnl]] – mRip4 catalytic domain (mutant) + staurosporine
**[[5wnk]] – mRip4 catalytic domain (mutant) + inhibitor
**[[5wni]] – mRip4 catalytic domain (mutant) + ATP
**[[6gwm]] – rRip2 caspase recruitment domain 433-539
*'''Ulk'''
**[[6qas]] – hChk Ulk1 + inhibitor
**[[5ci7]], [[6mnh]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[8soi]], [[8sqz]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein
**[[8srm]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein – Cryo EM
**[[8srq]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein + PI3K – Cryo EM
**[[6qav]], [[6qau]], [[6qat]], [[6yid]] – hChk Ulk2 + inhibitor
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[6fdz]], [[6fdy]] – hChk Ulk3 + leukemia drug
**[[6tsz]] – hChk Ulk4 pseudfokinase domain + ATPgS
**[[6u5l]] – hChk Ulk4 (mutant) + inhibitor
*'''Hipa''' and '''Hipb'''
**[[3tpd]], [[3tpe]] – EcChk Hipa – ''Escherichia coli''
**[[3tpb]], [[3dnt]], [[3dnu]] – EcChk Hipa (mutant)
**[[4pu7]], [[4pu8]] – SoChk Hipb - ''Shewanella oneidensis''
**[[3tpt]] – EcChk Hipa (mutant) + ADP
**[[3fbr]] – EcChk Hipa (mutant) + AMPPNP + peptide
**[[3tpv]] – EcChk Hipa + ADP
**[[2wiu]] – EcChk Hipa + Hipb
**[[4yg7]], [[5k98]], [[3hzi]], [[3dnv]] – EcChk Hipa + Hipb + DNA
**[[4yg1]], [[4z58]], [[4z59]], [[4z5c]], [[4z5d]] – EcChk Hipb + DNA
**[[4z5h]] – EcChk Hipb (mutant) + DNA
**[[4pu3]], [[4pu4]] – SoChk Hipa + Hipb + DNA - ''Shewanella oneidensis''
**[[4pu5]] – SoChk Hipa + AMPPNP
*'''Chk Smg'''
**[[6l53]] – hChk Smg1 – Cryo EM
**[[7pw6]] – hChk Smg1 + inhibitor – Cryo EM
**[[7pw7]] – hChk Smg1 + Smg9 + inhibitor – Cryo EM
**[[7pw9]] – hChk Smg1 + Smg9 + AMPPNP + ATP – Cryo EM
**[[6l54]], [[6syt]] – hChk Smg1 + Smg8 + Smg9 – Cryo EM
**[[7pw4]], [[7pw5]] – hChk Smg1 + Smg8 + Smg9 + inhibitor – Cryo EM
**[[7pw8]] – hChk Smg1 + Smg8 + Smg9 + AMPPNP – Cryo EM
**[[6z3r]] – hChk Smg1 + Smg8 + Smg9 + regulator of nonsense transcripts – Cryo EM
**[[2hwy]] – hChk Smg5 PIN domain
**[[2hww]], [[2hwx]] – hChk Smg6 PIN domain (mutant)
**[[4um2]] – hChk Smg6 TPR domain
**[[1ya0]] – hChk Smg7 N terminal
*'''Chk Vprbp or DCAF1'''
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain 1039-1401 (mutant)
**[[7sse]], [[7ufv]], [[8f8e]], [[8og5]], [[8og6]], [[8og7]], [[8og8]], [[8og9]], [[8oga]], [[8ogb]], [[8ogc]], [[8oo5]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) + inhibitor
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[5aja]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
*'''Other Chk'''
**[[1wak]] – hChk Sprk1
**[[3dak]] – hChk Osr1 kinase domain
**[[7okw]] – hChk Osr1 C-terminal
**[[4aw2]] – hChk Mrckα kinase domain
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain (mutant)
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[1uf0]] – hChk Dcamkl1 DCX domain – NMR
**[[1u5q]] – rChk Tao2 kinase domain
**[[2cos]] – mChk Lats2 – NMR
**[[1xte]], [[1xtn]], [[6edx]] – mChk Sgk3 PX domain
**[[4yom]] – mChk Brsk2
**[[4ynz]] – mChk Brsk1 N terminal domain
**[[5iri]] – mChk Brsk1 residues 592-719
**[[5oat]], [[7mp8]] – rfbChk Pink1– red flour beetle
**[[7t3x]] – Chk Pink1 (mutant) – louse
**[[4f0g]] – smChk Roco4 kinase domain – slime mold
**[[5tos]] – AtChk Bik1
**[[1q8z]], [[1zyc]] – yChk
**[[1how]], [[1zxe]], [[1zy4]] – yChk (mutant)
**[[1ow5]], [[1x9x]] – yChk Ste11 SAM domain – NMR
**[[2kio]], [[2kit]], [[1w1n]] – yChk Tor1 FATC domain – NMR
**[[3gre]] – yChk Vps15 WD repeat domain
**[[3osm]], [[3ost]] - yChk Kcc4 kinase domain
**[[5yyx]] – yChk Mek1 FHA domain
**[[6jxc]], [[6jxa]] – yChk Tel1 – Cryo EM
**[[6u69]] – CaChk Yck2 – ''Candida albicans''
**[[6sl1]], [[6sl0]], [[6skz]], [[6sky]] – Chk Tel1 – ''Chaetonium thermophilum'' – Cryo EM
**[[6ra0]] – CeChk Dkf1 – ''Chaenorhabditis elegans''
**[[7z6e]] – CeChk Mrck1 regulatory domain
**[[6tlb]] – Chk – ''Plasmodium falciparum''
*Other Chk complexes
**[[1wbp]], [[7dd1]] – hChk Sprk1 + peptide
**[[3beg]] – hChk Srpk1 + splicing factor SF2
**[[3hdm]], [[3hdn]], [[7pue]] – hChk Sgk1 (mutant) + inhibitor
**[[2r5t]] – hChk Sgk3 + AMPPNP
**[[4yff]], [[4yfi]], [[6b5j]], [[7mgj]], [[7mgk]] – hChk Tnni3k + inhibitor
**[[2v3s]] – hChk Osr1 + hChk Wnk4 peptide
**[[2vwi]] – hChk Osr1 kinase domain + ANP
**[[7que]], [[7quf]] – hChk Drak1 kinase domain + inhibitor
**[[4crs]] – hChk N2 kinase domain + ATPγS
**[[3tku]], [[4ual]], [[3qfv]], [[5ote]], [[5otf]] – hChk Mrckβ + inhibitor
**[[4uak]] – hChk Mrckβ + ADP
**[[5aja]], [[4z8l]], [[4cc9]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
**[[5jk7]] – hChk Vprbp WD repeat domain + VPX + DDB1 + UDG
**[[3wa0]], [[4p7i]] – hChk Vprbp residues 1417-1506 + merlin
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[5ci7]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[5b5w]], [[5b6b]], [[5brk]] – hChk Lats1 residues 622-704 + MOB1
**[[5yz0]] – hChk Atr + Atr-interacting protein – Cryo EM
**[[6bdn]] – hChk Tao3 kinase domain + ADP
**[[5yh3]] – hChk Fam20C 141-578 + pseudokinase Fam20A
**[[2gcd]] – rChk Tao2 kinase domain + staurosporine
**[[1u5r]] – rChk Tao2 kinase domain + ATP
**[[5yj9]], [[7mp9]] – rfbChk Pink1 kinase domain + AMPPNP
**[[6bn1]] – DmChk Hippo SARAH domain + Shar-Pei
**[[3hgk]] – Chk Pto + effector protein AVRPTOB – Currant tomato
**[[3p86]], [[3ppz]] - AtChk Ctr1 + staurosporine
**[[4f0f]] – smChk Roco4 kinase domain + APPCP
**[[4f1m]], [[4f1o]] – smChk Roco4 kinase domain (mutant) + APPCP
**[[4f1t]], [[4yzm]], [[4yzn]] – smChk Roco4 kinase domain + inhibitor
**[[5fvm]] - Tor2 + LST8 - ''Kluyveromyces marxianus''
**[[5kc2]] - yVps15 + Vps34 - Cryo EM
**[[5dfz]] - yVps15 + Vps34 + Vps30 + VPSAP28 + VPSAP30 - Cryo EM
**[[1q8y]], [[1q97]], [[1q99]], [[1zyd]] – yChk + nucleotide
**[[1zy5]] – yChk (mutant) + nucleotide
**[[2jd5]] – yChk + NPL-3P
**[[4lqs]], [[4lqq]], [[4lqp]] – yChk Cbk1 residues 251-756 + Cbk1 activator Mob2
**[[6emk]] – yChk Tor2 + LST8 + TSC11 + AVO1 + AVO2 – Cryo EM
**[[6s8f]] – yChk Tel1 + AMPPNP – Cryo EM
**[[5yyz]] – yChk Mek1 FHA domain + Hop1
**[[5x6o]], [[6z3a]], [[7wzr]], [[7wzw]]– yChk Mec1 + LCD1 – Cryo EM
**[[6z2w]], [[6z2x]] – yChk Mec1 (mutant) + LCD1 – Cryo EM
**[[7kue]] – yChk Kin28 in TFIIK complex – Cryo EM
**[[6u6a]] – CaChk Yck2 + inhibitor
**[[5fvm]] – Chk Tor2 + LST8 – ''Kluyveromyces maximanus''
*Serine/threonine protein kinase Rad53 see [[Rad53]]
*Serine/threonine protein kinase Gsk3B see [[Glycogen synthase kinase 3]]
}}
[[Category:Topic Page]]

Serine/threonine protein kinase 3D structures

2026-08-19T07:35:40Z

Michal Harel:

==3D structures of serine/threonine protein kinase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Chk1'''; domains - kinase 1-289; KA1 393-492
**[[1ia8]] – hChk1 kinase domain – human
**[[5w12]] – hChk1 KA1 domain
**[[1zlt]] – hChk1 kinase domain + hymenaldisine
**[[1nvq]], [[1nvr]] – hChk1 kinase domain + peptide + saurosporine
**[[1nvs]], [[1zys]], [[7ako]] - hChk1 kinase domain + peptide + inhibitor
**[[7akm]] - hChk1 kinase domain + ATP
**[[2ayp]], [[2br1]], [[2brb]], [[2brg]], [[2brh]], [[2brm]], [[2brn]], [[2bro]], [[2c3j]], [[2c3k]], [[2c3l]], [[2cgu]], [[2cgv]], [[2cgw]], [[2cgx]], [[2e9n]], [[2e9o]], [[2e9p]], [[2e9u]], [[2e9v]], [[2gdo]], [[2ghg]], [[2hog]], [[2hxl]], [[2hxq]], [[2hy0]], [[2qhm]], [[2qhn]], [[2r0u]], [[3f9n]], [[2wmq]], [[2wmr]], [[2wms]], [[2wmt]], [[2wmu]], [[2wmv]], [[2wmw]], [[2wmx]], [[2xey]], [[2xf0]], [[2xez]], [[2x8d]], [[2x8e]], [[2x8i]], [[2ydi]], [[2ydj]], [[2ydk]], [[2yer]], [[2yex]], [[2ym3]], [[2ym4]], [[2ym5]], [[2ym6]], [[2ym7]], [[2ym8]], [[2ywp]], [[3jvr]], [[3jvs]], [[3nlb]], [[3ot3]], [[3ot8]], [[3pa3]], [[3pa4]], [[3pa5]], [[3tkh]], [[3tki]], [[3u9n]], [[4fsm]], [[4fsn]], [[4fsq]], [[4fsr]], [[4fst]], [[4fsu]], [[4fsw]], [[4fsy]], [[4fsz]], [[4ft0]], [[4ft3]], [[4ft5]], [[4ft7]], [[4ft9]], [[4fta]], [[4ftc]], [[4fti]], [[4ftj]], [[4ftk]], [[4ftl]], [[4ftm]], [[4ftn]], [[4fto]], [[4ftq]], [[4ftr]], [[4ftt]], [[4ftu]], [[4gh2]], [[4hyh]], [[4hyi]], [[4jik]], [[4qye]], [[4qyf]], [[4qyg]], [[4qyh]], [[4rvk]], [[4rvl]], [[4rvm]], [[5dls]], [[5f4n]], [[5fcf]], [[5fck]], [[6fc8]], [[6fcf]], [[6fck]], [[7bko]], [[8e80]], [[8e81]] - hChk1 kinase domain + inhibitor 
**[[5oot]], [[5op2]], [[5op4]], [[5op5]], [[5op7]], [[5opb]], [[5opr]], [[5ops]], [[5opu]], [[5opv]], [[5oq5]], [[5oq6]], [[5oq7]], [[5oq8]], [[7bjd]], [[7bjh]], [[7bjj]], [[7bjm]], [[7bjo]], [[7bjr]], [[7bjx]], [[7bk1]], [[7bk2]], [[7bk3]], [[7mck]], [[7suf]], [[7sug]], [[7suh]], [[7sui]], [[7suj]], [[8siv]], [[8siw]], [[8six]] - hChk1 kinase domain (mutant) + inhibitor
**[[5oop]] - hChk1 kinase domain (mutant) + AMPPNP
**[[5oor]] - hChk1 kinase domain (mutant) + staurosporine
**[[7bkn]] - hChk1 kinase domain + adenine
**[[7bje]] - hChk1 kinase domain (mutant) + adenine
**[[2jqi]] – yChk1 – yeast
*'''Chk2 (Checkpoint kinase)'''
**[[1gxc]] – hChk2 phosphothreonine-binding domain + phosphopeptide
**[[2cn5]] – hChk2 kinase domain + ADP
**[[2cn8]] – hChk2 kinase domain + inhibitor
**[[2cn8]], [[2uv2]], [[2w0j]], [[2w7x]], [[2wtc]], [[2wtd]], [[2wti]], [[2wtj]], [[2xbj]], [[2xk9]], [[2xm8]], [[2xm9]], [[2ycf]], [[2ycq]], [[2ycr]], [[2ycs]], [[2yiq]], [[2yir]], [[2yit]], [[4a9r]], [[4a9s]], [[4a9t]], [[4bda]], [[4bdb]], [[4bdc]], [[4bdd]], [[4bde]], [[4bdf]], [[4bdg]], [[4bdh]], [[4bdi]], [[4bdj]], [[4bdk]] - hChk2 kinase domain + inhibitor
**[[3i6u]], [[3i6w]] – hChk2 residues 84-502 (mutant)
*'''Chk3 (Mst2)'''; domains - kinase 13-313; SARAH 436-484
**[[3wws]], [[4hkd]], [[4l0n]], [[4oh9]] – hChk3 SARAH domain 
**[[4lg4]] – hChk3 kinase domain
**[[4lgd]] – hChk3 kinase domain + RASSF5 SARAH domain
**[[6ao5]] – hChk3 kinase+SARAH domains (mutant) + SAV1 SARAH domain
**[[5dh3]], [[8a66]] – hChk3 kinase domain + inhibitor
*'''Chk4 (Mst1)''' ; Domains – kinase 1-311; SARAH 432-480
**[[3com]] – hChk4 kinase domain
**[[6yat]], [[8a5j]]– hChk4 kinase domain + inhibitor
**[[4nr2]] – hChk4 SARAH domain
**[[2jo8]] – hChk4 SARAH domain - NMR
**[[4oh8]] – hChk4 SARAH domain + Ras association domain-containing protein
*'''Chk5 (Aurora kinase b)'''
**[[4af3]] – hChk5 + inhibitor
*'''Chk6 or Chk15 or Aurora kinase A'''
**[[1mq4]], [[1muo]], [[4j8n]], [[4o0s]], [[6cpe]] – hChk6 kinase domain 
**[[4bn1]], [[4o0w]], [[4o0u]] – hChk6 kinase domain (mutant)
**[[5dnr]], [[5drd]], [[5dt3]] – hChk6 kinase domain + ATP
**[[5drd]] – hChk6 kinase domain + ATP
**[[1ol6]] – hChk6 kinase domain (mutant) + ATP
**[[2wqe]] – hChk6 kinase domain (mutant) + ADP
**[[5odt]] – hChk6 kinase domain (mutant) + ADP + TACC3
**[[2c6d]] – hChk6 kinase domain (mutant) + ADPNP
**[[2dwb]] – hChk6 kinase domain + AMPPNP
**[[6cpf]] – hChk6 kinase domain + AMPPCP
**[[5g15]] – hChk6 kinase domain + AMPPNP + monobody
**[[6cpg]], [[8ssp]] – hChk6 kinase domain + inhibitor + monobody
**[[2j4z]], [[2j50]], [[2np8]], [[2x81]], [[2x6d]], [[2x6e]], [[3efw]], [[3myg]], [[3vap]], [[3w10]], [[3w16]], [[3w18]], [[3w2c]], [[4b0g]], [[4byi]], [[4byj]], [[4j8m]], [[4jai]], [[4jaj]], [[4uyn]], [[4uzd]], [[4uzh]], [[4zs0]], [[4ztq]], [[4ztr]], [[4zts]], [[5aad]], [[5aae]], [[5aag]], [[5dpv]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5obr]], [[5one]], [[5zan]], [[6c2r]], [[6c2t]], [[6gra]], [[6z4y]], [[7ayh]], [[7ayi]], [[7fic]], [[7o2v]], [[8jmx]] – hChk6 kinase domain + inhibitor 
**[[2bmc]], [[2c6e]], [[2wtw]], [[2xne]], [[2xng]], [[2xru]], [[3coh]], [[3fdn]], [[3h0y]], [[3h0z]], [[3h10]], [[3lau]], [[3k5u]], [[3m11]], [[3nrm]], [[3p9j]], [[3r21]], [[3r22]], [[3qbn]], [[3unz]], [[3uo4]], [[3uo5]], [[3uo6]], [[3uod]], [[3uoh]], [[3uoj]], [[3uok]], [[3uol]], [[3up2]], [[3up7]], [[4dea]], [[4deb]], [[4ded]], [[4dee]], [[4dhf]], [[4jbo]], [[4jbp]], [[4jbq]], [[4prj]], [[5aad]], [[5aae]], [[5aaf]], [[5aag]], [[5dpv]], [[6hjj]], [[6hjk]] – hChk6 kinase domain (mutant) + inhibitor 
**[[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[5dos]], [[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5dn3]], [[5dos]], [[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[6c83]] – hChk6 kinase domain + AMPPCP + nanobody
**[[8sso]] – hChk6 kinase domain + drug + monobody
**[[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5g1x]], [[7ztl]] – hChk6 kinase domain (mutant) + N-Myc
**[[8guw]] – hChk6 kinase domain/activator peptide
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + Targeting protein for XKLP2
**[[3d14]], [[3d15]], [[3d2i]], [[3d2k]] [[3daj]], [[3dj5]], [[3dj6]], [[3dj7]] – Chk6 kinase domain (mutant) + inhibitor - mouse 
*Chk6 with phosphorylated Thr 287, Thr288
**[[1ol5]], [[1ol7]] – hChk6 kinase domain + PThr + ADP
**[[5dnr]], [[5dt3]] – hChk6 kinase domain + PThr + ATP
**[[2w1c]], [[2w1d]], [[2w1e]], [[2w1f]], [[2w1g]], [[5dn3]] – hChk6 kinase domain + PThr + inhibitor
**[[2wtv]], [[5orl]], [[5orn]], [[5oro]], [[5orp]], [[5orr]], [[5ors]], [[5ort]], [[5orv]], [[5orw]], [[5orx]], [[5ory]], [[5orz]], [[5os0]], [[5os1]], [[5os2]], [[5os3]], [[5os4]], [[5os5]], [[5os6]], [[5osd]], [[5ose]], [[5osf]] – hChk6 kinase domain (mutant) + PThr + inhibitor
**[[3e5a]], [[3ha6]] – hChk6 kinase domain + PThr + inhibitor + targeting protein for XKLP2
**[[5g1x]] – hChk6 kinase domain (mutant) + PThr + N-Myc
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + PThr + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + PThr + TPX2
**[[6r4a]], [[6r4b]], [[6r4c]], [[6r4d]] – hChk6 kinase domain + PThr + inhibitor + ADP
**[[6i2u]] – hChk6 kinase domain (mutant) + PThr + inhibitor + ADP
**[[6r49]] – hChk6 kinase domain (mutant) + PThr + CoA
*'''Chk10 (lymphocyte-oriented kinase)''' or LOK or STK10
**[[7qgp]] – hChk10
**[[2j7t]], [[4aot]], [[4equ]], [[4usd]], [[4use]], [[5ajq]], [[5owq]], [[5owr]], [[6eim]], [[6gtt]], [[6hxf]], [[6i2y]] – hChk10 kinase domain + inhibitor
**[[4bc6]], [[6i2y]] – hChk10 + drug
*'''Chk11'''
**[[2wtk]] – hChk11 (mutant) + calcium-binding protein
*'''Chk12-A (Aurora kinase b-a or Aurora B kinase)'''
**[[2vgo]], [[2vgp]], [[2vrx]], [[3ztx]], [[4c2v]], [[5eyk]] – fChk12-A + inner centromere protein A peptide + inhibitor - frog
**[[4c2w]] – fChk12-A + inner centromere protein A peptide + AMPPNP
**[[4b8l]], [[4b8m]], [[5k3y]] – fChk12-A (mutant) + inner centromere protein A peptide + inhibitor
*'''Chk13 (Polo-like kinase Plk)'''
*Plk1 Polo-box domain (Pbd) 371-594''
**[[1q4o]], [[2ogq]], [[3hih]], [[3p2w]], [[4h5x]], [[6n46]] – hPlk1 Pbd
*Plk1 Pbd complex with polypeptide
**[[1umw]], [[2ojx]], [[3bzi]], [[3c5l]], [[3rq7]], [[4dfw]], [[4rcp]], [[4o6w]], [[4o56]], [[4whh]], [[4whk]], [[4whl]], [[5dms]], [[5dmv]], [[5dnj]] , [[7mso]], [[7mx1]] – hPlk1 + peptide
**[[3hik]], [[3fvh]], [[3p2z]], [[3p34]], [[3p35]], [[3p36]], [[3p37]], [[3q1i]], [[4e67]], [[4e9c]], [[4e9d]], [[4hab]], [[4hy2]], [[4o9w]], [[4x9r]], [[4x9v]], [[4x9w]], [[5j19]], [[6gy2]] – hPlk1 + phosphopeptide
**[[1q4k]] – hPlk1 (mutant) + phosphopeptide
**[[2v5q]] – hPlk1 + design ankyrin repeat protein
**[[4lkl]] – hChk Plk1 + PL-55
**[[4lkm]] – hChk Plk1 + PL-74
**[[6ax4]] – hChk Plk1 + histidine cyclized macrocycle
**[[5x3s]] – mPlk1 + phosphopeptide
**[[8joq]], [[8joy]] – hPlk1 Pbd + hpv peptide
*Plk1 Pbd complex with small molecule inhibitor
**[[4h71]], [[4hco]], [[5ta6]], [[5ta8]], [[8bjt]], [[8crc]] – hPlk1 + inhibitor
**[[2rku]] – hPlk1 (mutant) + inhibitor
**[[3db6]], [[3db8]], [[3dbc]], [[3dbd]], [[3dbe]], [[3dbf]] – zfPlk1 (mutant) + inhibitor – zebra fish
*Plk1 catalytic domain 36-345
**[[2owb]] – hPlk1 catalytic domain (mutant)
**[[2ou7]] – hPlk1 catalytic domain (mutant) + AM
**[[2yac]], [[3kb7]], [[3thb]], [[4a4l]], [[4a4o]] – hPlk1 catalytic domain + inhibitor
**[[3fc2]] – hPlk1 catalytic domain (mutant) + inhibitor
**[[4j52]], [[4j53]] – hChk Plk1 (mutant) + inhibitor
**[[3d5x]] – zfPlk1 catalytic domain (mutant) + wortmannin
**[[3d5w]] – zfPlk1 catalytic domain + ADP
*'''Plk2'''
**[[4i5m]], [[4i5p]], [[4i6b]], [[4i6f]], [[4i6h]] – hChk Plk2 kinase domain (mutant) + inhibitor
**[[4rs6]], [[4xb0]] – hChk Plk2 Pbd
*'''Plk3'''
**[[4b6l]], [[4i6b]] – hChk Plk3 kinase domain + inhibitor
*'''Plk4'''; Domains – kinase 2-275; Pbd 580-808; Pb3 884-970
**[[3cok]] – hChk Plk4 kinase domain
**[[4n9j]] – hChk Plk4 Pbd domain
**[[4n7v]], [[4n7z]] – hChk Plk4 Pbd domain + centrosomal protein
**[[6w38]], [[6w3i]] – hChk Plk4 Pbd domain + Fam46C
**[[6w3j]] – hChk Plk4 Pbd domain + Fam46C + CEP92 peptide
**[[4jxf]], [[4yur]] – hChk Plk4 kinase domain + inhibitor
**[[5lhy]] – hChk Plk4 Pb3 domain
**[[4yyp]], [[5lhz]] – hChk Plk4 Pb3 domain + Scl-interrupting locus protein
**[[4g7n]], [[4nk7]], [[5lhx]], [[7rl3]] – DmChk Plk4 Pbd domain – ''Drosophila melanogaster''
*'''Chk16'''
**[[2buj]] – hChk16 (mutant) + staurosporin
*'''Chk17B''' or DRAK2 or STK17B
**[[3lm0]] – hChk17B
**[[6qf4]], [[7q7c]], [[7q7d]] – hChk17B + ADP
**[[7q7e]] – hChk17B + ATP
**[[3lm5]] – hChk17B + quercetin
**[[6y6f]], [[6y6h]], [[6zjf]] – hChk17B + pyrimidine derivative
**[[7akg]] – hChk17B + drug
*'''Chk19''' or STK19
**[[7xrb]] – hChk19
*'''Chk24 (Mst3)''' or STK24
**[[3a7f]], [[3a7g]], [[3a7h]], [[3a7i]], [[3a7j]], [[3ckw]] – hChk24 kinase domain
**[[4w8e]], [[4w8d]], [[4u8z]], [[4qmm]], [[4qmn]], [[4qmo]], [[4qmp]], [[4qmq]], [[4qms]], [[4qmt]], [[4qmu]], [[4qmv]], [[4qmw]], [[4qmx]], [[4qmy]], [[4qmz]], [[4qna]], [[4qo9]], [[4u8z]], [[7b30]], [[7b31]], [[7b32]], [[7b33]], [[7b34]], [[7b35]], [[8bzi]], [[8bzj]], [[8qlr]], [[8qls]], [[8qlt]] – hChk Mst3 + inhibitor
**[[8qlq]] – hChk Mst3 + macrocyclic inhibitor
**[[3ckx]] – hChk24 kinase domain + staurosporin
**[[3zhp]] – hChk24 kinase domain + calcium-binding protein
**[[4o27]] – hChk24 kinase domain (mutant) + calcium-binding protein
**[[4qml]] – hChk Mst3 kinase domain + AMPPNP
*'''Chk25 or STK25'''
**[[2xik]] – hChk25 kinase domain
**[[7z4v]] – hChk25 kinase domain + inhibitor
**[[3w8h]] – hChk25 regulatory domain + programmed cell death protein 10
**[[4nzw]] – hChk25 kinase domain (mutant) + calcium-binding protein
*'''Chk26 (Mst4)'''
**[[3ggf]], [[7b36]] – hChk Mst4 + inhibitor
**[[4geh]], [[3w8i]] - hChk Mst4 dimerization domain + programmed cell death protein 10
**[[4fza]], [[4fzd]], [[4fzf]] – hChk Mst4 (mutant) + calcium-binding protein
*'''Chk32'''
**[[4fr4]] – hChk32A
*'''Chk38'''
**[[6bxi]] – hChk38 kinase domain
*'''Chk39''' or SPAK
**[[7o86]] – hChk39 C-terminal
**[[5d9h]] – mChk39 residues 63-403 + ATP
**[[5dbx]] – mChk39 residues 63-403 (mutant) + AMPPNP
*'''Chk40'''
**[[5l2q]] – hChk40 kinase homology domain
*'''Dclk1'''
**[[6kyq]] – hChk Dclk1 kinase domain
**[[6kyr]] – hChk Dclk1 kinase domain (mutant)
**[[5jzj]] – hChk Dclk1 kinase domain + AMPPN
**[[5jzn]], [[7kx6]], [[7kxw]] – hChk Dclk1 kinase domain + inhibitor
**[[7f3g]] – hChk Dclk1 kinase domain + drug
**[[7kx8]] – hChk Dclk1 C-terminal + inhibitor
*'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123; kinase 144-480
**[[1unp]], [[1unr]] – hRac-α hChk pleckstrin homology domain
**[[2uzr]], [[2uzs]], [[7myx]] – hRac-α hChk pleckstrin homology domain (mutant)
**[[1h10]], [[1unq]], [[2uvm]] – hRac-α hChk pleckstrin homology domain + inositol tetrakisphosphate
**[[3o96]], [[4ejn]], [[6s9w]], [[6s9x]], [[6hhj]], [[6hhi]], [[6hhh]], [[6hhg]], [[6hhf]] - hRac-α hChk + inhibitor
**[[5kcv]], [[7nh4]], [[7nh5]] - hRac-α hChk (mutant) + inhibitor
**[[4gv1]], [[4ekl]] - hRac-α hChk kinase domain + inhibitor
**[[3qkm]], [[6ccy]] - hRac-α hChk kinase domain (mutant) + inhibitor
**[[6buu]] - hRac-α hChk kinase domain + bisubstrate peptide
**[[4ekk]] - hRac-α hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[6npz]] - hRac-α hChk kinase domain + peptide + inhibitor
**[[3ow4]], [[3qkk]], [[3qkl]], [[6buu]] - hRac-α hChk kinase domain (mutant) + peptide + inhibitor
**[[7apj]] - hRac-α hChk + nanobody
*'''Rac-β hChk (AKT2)'''
**[[1gzk]], [[1gzn]], [[1gzo]], [[1mrv]], [[1mry]] – hRac-β hChk kinase domain
**[[1p6s]] - hRac-β hChk pleckstrin homology domain - NMR
**[[1o6k]] - hRac-β hChk kinase domain + GSK3 peptide + AMPPNP
**[[2jdo]], [[2jdr]], [[2uw9]], [[2x39]], [[3cqu]], [[3cqw]] - hRac-β hChk kinase domain + GSK3 peptide + inhibitor
**[[3e87]], [[3e88]], [[3e8d]] - Rac-β hChk kinase domain (mutant) + GSK3 peptide + inhibitor<br /
**[[1o6l]] - hRac-β hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[3d0e]], [[8q61]] - hRac-β hChk kinase domain (mutant) + inhibitor
*'''Rac-γ hChk (ATK3)'''
**[[2x18]] – Rac-γ hChk PH domain
*'''A-Raf'''
**[[1wxm]] – hA-Raf RAS-binding domain 19-91 - NMR
**[[2mse]] – hA-Raf RAS-binding domain + APOA-I + K-ras - NMR
*'''B-Raf'''; domains - BRS 38-116; Ras-binding 153-237; kinase 445-723
**[[8dgs]], [[8dgt]] – hB-Raf in Ras/Raf complex – Cryo EM
**[[7z37]], [[7z38]], [[7zr5]] – hB-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
**[[1uwh]], [[3c4c]], [[6v2u]], [[6xfp]], [[6xlo]], [[8f7o]], [[8f7p]] – hB-Raf kinase domain + anticancer drug
**[[1uwj]], [[6p3d]] – hB-Raf kinase domain (mutant) + anticancer drug
**[[2fb8]], [[3d4q]], [[3ii5]], [[3psd]], [[3skc]], [[3tv6]], [[4g9c]], [[4ksp]], [[4ksq]], [[3psb]], [[3ppj]], [[3ppk]], [[3prf]], [[3pri]], [[3tv4]], [[4dbn]], [[4e4x]], [[4mbj]], [[4ehe]], [[3q4c]], [[3q96]], [[3e26]], [[4h58]], [[4e26]], [[4fc0]], [[4pp7]], [[6cad]], [[7shv]] – hB-Raf kinase domain + pyrazole inhibitor
**[[4jvg]], [[4ehg]], [[4fk3]], [[3idp]], [[4g9r]], [[4wo5]], [[4mnf]], [[4r5y]], [[4rzv]], [[4rzw]], [[4xv1]], [[4xv2]], [[4xv3]], [[4xv9]], [[4yht]], [[5c9c]], [[5hi2]], [[5ita]], [[5jrq]], [[5jsm]], [[5jt2]], [[6nsq]], [[6p7d]], [[6uuo]] – hB-Raf kinase domain (mutant) + pyrazole inhibitor
**[[5csw]], [[5csx]], [[5ct7]], [[5fd2]], [[5hid]], [[5hie]], [[5val]], [[5vam]], [[6b8u]], [[6n0q]], [[6n0p]], [[7k0v]], [[7p3b]], [[7p3v]], [[8c7x]], [[8c7y]] - hB-Raf kinase domain + inhibitor
**[[6v34]] – hB-Raf kinase domain (mutant) + inhibitor
**[[4mne]] – hB-Raf kinase domain + MAPKK1
**[[8f7o]] – hB-Raf kinase domain + drug
**[[7m0u]] – hB-Raf kinase domain + AMPPNP + drug
**[[6u2h]] – hB-Raf kinase domain + 14-3-3 ζ/δ
**[[7mfe]] – hB-Raf + 14-3-3 ζ/δ – Cryo EM
**[[7mff]] – hB-Raf + 14-3-3 ζ/δ + inhibitor – Cryo EM
**[[7mfd]] – hB-Raf + 14-3-3 ζ/δ + MEK + inhibitor – Cryo EM
**[[6pp9]] – hB-Raf kinase domain + MEK1 + ANP
**[[7m0x]], [[7m0z]] – hB-Raf kinase domain + MEK1 + ANP + inhibitor
**[[7m0t]], [[7m0u]], [[7m0v]], [[7m0w]], [[7m0y]] – hB-Raf kinase domain + MEK1 + ANP + drug
**[[6u2g]] – hB-Raf kinase domain + MEK1 + AMPPCP
**[[5vr3]] – hB-Raf BRS domain
**[[7jhp]] – hB-Raf BRS domain + Hras
**[[6ntc]], [[6ntd]] – hB-Raf BRS domain (mutant) + Hras
**[[6xi7]] – hB-Raf 52-188 + Kras
**[[2l05]], [[5j17]], [[5j2r]] – hB-Raf RAS-binding domain - NMR
**[[3ny5]] – hB-Raf RAS-binding domain
**[[5j18]] – hB-Raf RAS-binding domain + inhibitor - NMR
**[[6pts]], [[6ptw]] – hB-Raf 56-187 + Kras + apolipoprotein + GMPPNP - NMR
**[[6uan]], [[6q0k]] – hB-Raf + 14-3-3 ζ – Cryo EM
**[[6nyb]] – hB-Raf + 14-3-3 ζ + MEK1 – Cryo EM
**[[6q0t]], [[6q0j]] – hB-Raf (mutant) + 14-3-3 ζ + MEK1 – Cryo EM
*'''c-Raf'''; Domains – RAS-binding (RBD) 55-132; Cys-rich 136-187 (CBD); kinase 323-618
**[[1rfa]], [[8jna]], [[8jof]], [[8jog]] – hc-Raf RBD - NMR
**[[1faq]], [[1far]] – hc-Raf cysteine-rich domain - NMR
**[[3omv]] – hc-Raf kinase domain
**[[1rrb]] – c-Raf RBD – NMR - rat
*c-Raf complex with protein
**[[8cpd]] – hc-Raf + 14-3-3 protein zeta – Cryo EM
**[[9mmp]] – hc-Raf + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[9mmr]] – hc-Raf (mutant) + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[1c1y]] – hc-Raf RBD + RAP1A
**[[3kuc]] – hc-Raf RBD (mutant) + RAP1A
**[[1gua]] – hc-Raf RBD + RAP1A + GPPNHP
**[[8jnb]] – hc-Raf RBD + ligand
**[[4g0n]], [[4g3x]] – hc-Raf RBD + GTPase Hras
**[[3kud]] – hc-Raf RBD (mutant) + GTPase Hras
**[[8epw]], [[8t74]] – hc-Raf RBD + GTPase K-ras
**[[8t75]], [[9ygs]] – hc-Raf RBD-CRD + GTPase K-ras + GMPPNP
**[[9ay7]], [[9aya]] – hc-Raf + MEK1
**[[9mmq]] – hc-Raf + MEK1 – Cryo EM
**[[9mms]] – hc-Raf (mutant) + MEK1 – Cryo EM
**[[9o0u]], [[9o0v]] – hc-Raf (mutant) + MEK1 + ANP + inhibitor– Cryo EM
**[[8u1l]] – hc-Raf + Hsp90 + CDC37 – Cryo EM
**[[8gae]], [[8gft]] – hc-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
*'''Snf1-related Chk'''
**[[3uc4]], [[3uc3]], [[3udb]], [[3zut]], [[3zuu]] – AtChk Srk2E kinase domain (mutant) – ''Arabidopsis thaliana''
**[[3ujg]] – AtChk Srk2E kinase domain (mutant) + protein phosphatase 2C
**[[5yks]] – hChk
*'''MAPK-interacting Chk''' or Mnk1 Mnk2
**[[2hw6]] – hMnk 1 catalytic domain
**[[2hw7]] – hMnk 1 catalytic domain + staurosporin
**[[5wvd]] – hMnk 1 catalytic domain + inhibitor
**[[2ac3]] – hMnk 2 catalytic domain
**[[2ac5]] – hMnk 2 catalytic domain (mutant)
**[[6cj5]], [[6cje]], [[6cjh]], [[6cjw]], [[6cjy]], [[6ck3]], [[6ck6]], [[6cki]] – hMnk 2 catalytic domain (mutant) + inhibitor
*'''hChk Pak''' or '''Chk N''' or '''PRK1'''; Domains - CRIB 74-109; Hr1B 122-199; catalytic 109-426; kinase 605-942
**[[1urf]] – hChk Pak-1 Hr1b domain - NMR
**[[4nkg]] – hChk Pak-1 Hr1b domain + SSPH1 LRR domain
**[[2rmk]] – hChk Pak-1 Hr1bb domain + Rac1 - NMR
**[[1f3m]] – hChk Pak-1 autoregulatory+kinase domains
**[[4otd]] - hChk Pak-1 kinase domain
**[[1yhv]], [[1yhw]], [[3q4z]], [[3q52]], [[3q53]] – hChk Pak-1 kinase domain (mutant)
**[[4o0r]], [[4o0t]], [[4zji]], [[4zjj]], [[4zlo]], [[4zy4]], [[4zy5]], [[4zy7]], [[5ime]], [[5kbq]], [[5kbr]], [[6b16]], [[7vto]] – hChk Pak-1 kinase domain + inhibitor
**[[4oti]], [[4oth]], [[4otg]] – hChk Pak-1 kinase domain + inhibitor
**[[4eqc]], [[4p90]], [[5dew]], [[5dey]], [[5dfp]] – hChk Pak-1 kinase domain (mutant) + inhibitor
**[[2hy8]] – hChk Pak-1 kinase domain + staurosporin
**[[2qme]] – hChk Pak-1 CRIB domain + RAC3
**[[3fxz]], [[3fy0]], [[4daw]] – hChk Pak-1 kinase domain (mutant) + Ru complex
**[[6fd3]] – hChk Pak-3 kinase domain (mutant)
**[[2j0i]], [[4fie]] – hChk Pak-4
**[[4fig]], [[4fij]], [[4l67]] – hChk Pak-4 kinase domain
**[[2cdz]] – hChk Pak-4 + purine derivative
**[[2ov2]] – hChk Pak-4 CRIB domain + RAC3
**[[2qon]], [[4fif]], [[4fih]], [[4fii]], [[4jdh]], [[4jdi]], [[4jdj]], [[4jdk]], [[6wlx]], [[6wly]] – hChk Pak-4 kinase domain + peptide
**[[4app]], [[4o0v]], [[4o0x]], [[4o0y]], [[4njd]], [[4xbu]], [[5bms]], [[5i0b]], [[5vee]], [[5vef]], [[5zjw]], [[5xvg]], [[5xvf]], [[5xva]], [[7cmb]], [[7cp3]], [[7cp4]] – hChk Pak-4 kinase domain + inhibitor
**[[2x4z]], [[2xh5]] – hChk Pak-4 kinase domain (mutant) + inhibitor
**[[5upl]], [[5upk]] – hChk Pak-4 kinase domain (mutant) + CDC42
**[[5ved]] – hChk Pak-4 kinase domain + staurosporine
**[[8ahi]] – hChk Pak-4 300-591 + inhibitor
**[[7s46]], [[7s48]] – hChk Pak-4 catalytic domain + integrin beta-5 peptide
**[[2c30]] – hChk Pak-6
**[[2odb]] – hChk Pak-6 CRIB domain + CDC42
**[[4ks8]] – hChk Pak-6 kinase domain + sunitinib
**[[4ks7]] – hChk Pak-6 kinase domain (mutant) + inhibitor
**[[2f57]] – hChk Pak-7
*'''Mycobacterium tuberculosis Chk Pkn'''
**[[4x3f]] - MtChk PknA – ''Mycobacterium tuberculosis''
**[[4ow8]] - MtChk PknA kinase domain
**[[3ori]], [[3ork]], [[3orl]], [[3orm]], [[3oro]], [[3orp]], [[3ort]] - MtChk PknB kinase domain (mutant)
**[[1o6y]] – MtChk PknB kinase domain
**[[6b2p]], [[6b2q]] – MtChk PknB kinase domain + inhibitor
**[[2kud]], [[2kue]], [[2kuf]], [[2kui]] – MtChk PknB pasta domains 2-3 - NMR
**[[3ouv]] – MtChk PknB pasta domain 3
**[[5e0y]] – MtChk PknB pasta domain 4
**[[5e10]] – MtChk PknB pasta domains 1-2
**[[5e0z]] – MtChk PknB pasta domains 3-4
**[[5e12]] – MtChk PknB pasta domains 2-4
**[[5u94]] - MtChk PknB kinase domain + inhibitor
**[[3f61]], [[3f69]] - MtChk PknB kinase domain (mutant) + inhibitor
**[[6i2p]] - MtChk PknB kinase domain (mutant) + GARA + peptide
**[[1rwi]], [[1rwl]] - MtChk PknD extracellular domain
**[[2h34]] – MtChk PknE catalytic domain
**[[7naa]] – MtChk PknF kinase domain + inhibitor
**[[4y12]] - MtChk PknG + ATP-gS
**[[4y0x]] - MtChk PknG + ADP
**[[7q52]] - MtChk PknG + inhibitor
**[[4esq]] - MtChk PknH extracellular domain
**[[5m06]], [[5xka]] - MtChk PknI kinase domain
**[[5m07]], [[5m08]], [[5m09]] - MtChk PknI kinase domain (mutant)
**[[5xlm]], [[5xll]] - MtChk PknI sensor domain
**[[7mxb]], [[7mxj]], [[7mxk]] - Chk PknG kinase domain + AMPPNP - Corynebacterium glutamicum
*'''hChk Nek'''
**[[4apc]] – hChk Nek1 kinase domain (mutant)
**[[4b9d]] - hChk Nek1 kinase domain (mutant) + inhibitor
**[[2w5h]] – hChk Nek2 kinase domain
**[[2jav]], [[2wqo]], [[2xk3]], [[2xk4]], [[2xk6]], [[2xk7]], [[2xk8]], [[2xkc]], [[2xkd]], [[2xke]], [[2xkf]], [[2xnm]], [[2xnn]], [[2xno]], [[2xnp]], [[4a4x]], [[4afe]], [[5m51]], [[5m53]], [[5m55]], [[5m57]], [[6sgd]], [[6sgh]], [[6sgi]], [[6sgk]], [[6sk9]] – hChk Nek2 + inhibitor
**[[2w5a]], [[2w5b]] – hChk Nek2 + nucleotide
**[[6tm5]] - hChk Nek2 in anaphase-promoting complex – Cryo EM
**[[2wqm]], [[6s76]] – hChk Nek7
**[[2wqn]] – hChk Nek7 + ADP
**[[5de2]] – hChk Nek7 + hChk Nek9
**[[6s73]], [[2wqo]] – hChk Nek7 + inhibitor
**[[6npy]] – hChk Nek7 + Nlrp3
**[[6s75]] – hChk Nek7 + inhibitor
*'''Chk Rio'''
**[[6fdo]], [[6fdn]], [[6fdm]] – hChk Rio2
**[[4otp]] – hChk Rio1 Rio domain + ADP
**[[6hk6]], [[7vbt]] – hChk Rio2 + inhibitor
**[[6eml]], [[6fai]], [[6g18]], [[6g51]], [[6rbd]],[[6rbe]], [[6y7c]] – yChk Rio2 in 40S particle – Cryo EM
**[[1ztf]] – AfChk Rio1 + adenine derivative – Archaeoglobus fulgidus
**[[1zth]] – AfChk Rio1 + ADP
**[[1zp9]] – AfChk Rio1 + ATP
**[[1tqp]], [[1zao]] – AfChk Rio2 + ATP
**[[1zar]] – AfChk Rio2 + ADP
**[[4gyg]] – CtChk Rio2 – Chaetonium thermophilum
**[[4gyi]] – CtChk Rio2 + ADP
*hChk Vrk (vaccinia-related kinase)
**[[2kty]], [[2kul]], [[2lav]], [[2rsv]] – hChk Vrk1 kinase domain 1-396 - NMR
**[[3op5]] – hChk Vrk1 kinase domain (mutant)
**[[5ukf]] – hChk Vrk1 kinase domain + inhibitor
**[[5uvf]], [[6cnx]], [[6bu6]], [[6cfm]], [[6dd4]], [[6bp0]], [[6bru]], [[6btw]], [[6cmm]], [[6cqh]], [[6csw]], [[6npn]], [[6vxu]], [[6vzh]] – hChk Vrk1 kinase domain (mutant) + inhibitor
**[[6ac9]] – hChk Vrk1 kinase domain (mutant) + AMPPNP
**[[7tan]] – hChk Vrk1 kinase domain + nucleosome – Cryo EM
**[[2v62]] – hChk Vrk2 kinase domain
**[[5uu1]], [[6ncg]], [[8q1z]] – hChk Vrk2 kinase domain + inhibitor
*Chk Wnk (protein kinase lysine-deficient); Domains - kinase 194-483; CCT1 454-549
**[[6cn9]], [[4q2a]], [[4pwn]] - hChk Wnk1 kinase domain (mutant)
**[[5tf9]] - hChk Wnk1 kinase domain + inhibitor + AMPPNP
**[[5wdy]], [[5we8]] - hChk Wnk1 kinase domain + inhibitor + ANP
**[[5drb]], [[6ol2]]- rChk Wnk1 kinase domain (mutant) + inhibitor
**[[6elm]] - hChk Wnk2 CCT1 domain
**[[6fbk]] - hChk Wnk2 CCT1 domain + Wnk1 peptide
**[[5o1v]], [[5o21]], [[5o23]] - hChk Wnk3 kinase domain
**[[5o2c]] - hChk Wnk3 kinase + CCT1 domains
**[[5o26]], [[5tf9]] - hChk Wnk3 kinase domain + AMPPNP
**[[5o2b]] - hChk Wnk3 kinase domain + inhibitor
**[[8edh]] - hChk Wnk3 kinase domain (mutant) + inhibitor
**[[2lru]] – rChk Wnk1 autoinhibitory domain 480-572 - NMR
**[[5w7t]] - rChk Wnk1 kinase domain
**[[7uos]] - rChk Wnk1 kinase domain (mutant)
*'''TANK-binding kinase'''
**[[4efo]] – hChk Tbk1 ubiquitin-like domain
**[[6rsr]], [[6rsu]] – hChk Tbk1 + inhibitor
**[[4im0]], [[4im2]], [[4im3]], [[4iw0]], [[4iwo]], [[4iwp]], [[4ipq]], [[6rst]] – hChk Tbk1 (mutant) + inhibitor
**[[6cq5]], [[6cq4]], [[6cq0]], [[6boe]], [[6bod]], [[6bny]], [[5w5v]] – hChk Tbk1 + ulcer drug
**[[4eut]], [[4euu]] – hChk Tbk1 kinase+ubiquitin-like domains (mutant) + inhibitor
**[[6nt9]] – hChk Tbk1 (mutant) + STING
**[[5eoa]], [[5eof]] – hChk Tbk1 residues 677-729 + optineurin
**[[4jl9]], [[4jlc]] – mChk Tbk1 + inhibitor
**[[6o8c]], [[6o8b]] – mChk Tbk1 (mutant) + STING
*'''Haspin'''
**[[2vuw]], [[2wb8]] – hChk Haspin kinase domain
**[[3dle]] – hChk Haspin kinase domain + AMP
**[[3e7v]], [[3f2n]], [[3fmd]], [[3iq7]], [[4qtc]], [[5htb]], [[5htc]], [[6z56]], [[6z57]], [[6z58]], [[6z59]], [[6z5a]], [[6z5b]], [[6z5c]]. [[6z5d]], [[6z5e]] , [[7avq]], [[7ops]] – hChk Haspin kinase domain + inhibitor
**[[7sqm]] – hChk Haspin kinase domain + antimalarial
**[[6g38]], [[6g34]], [[6g35]], [[6g36]], [[6g37]] – hChk Haspin kinase domain + tubercidin derivative
**[[6g39]], [[6g3a]] – hChk Haspin kinase domain (mutant) + tubercidin derivative
**[[4ouc]] – hChk Haspin kinase domain + histone H3 peptide
*'''MAP/microtubule affinity-regulating kinase (MARK)'''
**[[2hak]] – hChk MARK1 catalytic+UBA domains
**[[3ose]] - hChk MARK1 KA1 domain
**[[6c9d]] – hChk MARK1 catalytic+UBA+KA1 domains (mutant)
**[[5eak]], [[5kz7]], [[5kz8]] – hChk MARK2 catalytic+UBA domains + inhibitor
**[[3iec]] – hChk MARK2 catalytic+UBA domains + cytotoxicity-associated immunodominant antigen peptide
**[[2qnj]] – hChk MARK3 catalytic+UBA domains
**[[3fe3]] – hChk MARK3 catalytic+UBA domains (mutant)
**[[7p1l]] – hChk MARK3 catalytic+UBA domains + inhibitor
**[[5es1]] – hChk MARK4 catalytic+UBA domains + inhibitor
**[[1zmu]] – rChk MARK2 catalytic+UBA domains
**[[2wzj]], [[2r0i]], [[1zmv]], [[1y8g]], [[1zmw]] – rChk MARK2 catalytic+UBA domains (mutant)
**[[1ul7]], [[1v5s]] - mChk MARK3 catalytic domain - NMR
*'''Mitotic checkpoint Chk (Bub)'''; Domains: TPR 1-220; kinase 726-1085
**[[2lah]] – hChk Bub1 TPR domain – NMR
**[[2wvi]] – hChk Bub1β TPR domain
**[[3si5]] – hChk Bub1 TPR domain + CASC5 peptide
**[[4r8q]], [[4qpm]], [[5dmz]] – hChk Bub1 kinase domain + ADP
**[[6f7b]] – hChk Bub1 kinase domain + inhibitor
**[[4a1g]] – hChk Bub1 TPR domain + CASC5 KI motif
**[[4ggd]] - hChk Bub1 + cell division cycle protein
**[[6tlj]], [[5khu]] - hChk Bub1 in anaphase-promoting complex – Cryo EM
**[[6jkk]] – DmChk Bub1 kinase domain
**[[6jkm]] – DmChk Bub1 kinase domain + ADP
**[[5jja]] – hChk Bub1 residues 661-734 + PP2A
**[[3esl]] – yChk Bub1 N terminal
**[[4bl0]] - yChk Bub1 + cell cycle arrest protein Bub3
*'''Microtubule-associated Chk'''
**[[2m9x]] – hChk 1 residues 187-287 – NMR
**[[3ps4]] - hChk 1 residues 965-1057
**[[2kqf]], [[2kyl]] – hChk 2 PDZ domain + glycoprotein C terminal – NMR
**[[3khf]] - hChk 3 PDZ domain
**[[2w7r]] – hChk 4 PDZ domain
*'''mTOR''' or '''Mechanistic target of rapamycin'''
*''mTOR FRB domain residues 2015-2114''
**[[1nsg]], [[1fap]] – hFRAP FRB domain + FKBP
**[[2rse]] – hFRAP FRB domain + FKBP – NMR
**[[1aue]] – hFRAP FRB domain
**[[2gaq]], [[2npu]] – hFRAP FRB domain - NMR
**[[8ppz]] – hFRAP FRB domain + FKBP + pyridine derivative
**[[3fap]], [[2fap]], [[4fap]] – hFRAP FRB domain + FKBP + rapamycin analog
**[[4drh]], [[4dri]], [[4drj]], [[5gpg]] – hFRAP FRB domain + FKBP + rapamycin
**[[6m4u]], [[6m4w]] – hChk Mtor FRB domain (mutant) + FKBP1A + rapamycin
**[[5wbh]] – hFRAP FRB domain + S6K1 peptide
*''mTOR FAT+PIKK domain residues 1376-2549''
**[[4jsn]] – hFRAP + TORC subunit LST8
**[[4jsp]] – hFRAP + TORC subunit LST8 + ATP
**[[4jsv]] – hFRAP + TORC subunit LST8 + ADP
**[[4jsx]] – hFRAP + TORC subunit LST8 + torin2
**[[4jt5]] – hFRAP + TORC subunit LST8 + pp242
**[[4jt6]] – hFRAP + TORC subunit LST8 + PI-103
**[[5wby]], [[5wbu]] – hFRAP + TORC subunit LST8 + proline-rich Akt1 substrate
*''mTOR complex''
**[[5flc]] – hmTOR + RAPTOR + LST8 + FKBP – Cryo EM
**[[5h64]] – hmTOR + RAPTOR + LST8 – Cryo EM
**[[6sb2]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC – Cryo EM
**[[6sb0]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC + proline-rich Akt1 substrate – Cryo EM
**[[5zcs]] – hmTOR + LST8 + AVO3 + TORC2 – Cryo EM
**[[7tzo]] – hTORC2 in mTORC2 complex– Cryo EM
**[[6zwm]], [[6zwo]], [[7owg]], [[7pe7]], [[7pe8]], [[7pe9]], [[7pea]], [[7peb]], [[7pec]], [[7uxc]] , [[8era]]– mTOR in mTor complex – Cryo EM
*'''Gcn2'''
**[[1zyc]] – yChk Gcn2
**[[1zxe]], [[1zy4]], [[1zy5]] – yChk Gcn2 (mutant)
**[[2yz0]] – yChk Gcn2 RWD/GI domain – NMR
**[[4otm]] – yChk Gcn2 C terminal domain
**[[1zyd]] – yChk Gcn2 + ATP
**[[4otn]] – mChk Gcn2 C terminal domain
*'''LRRK1''' or leucine-rich repeat Chk1
**[[8e04]], [[8e05]], [[8e06]], [[8fac]] – hLRRK1 – Cryo EM
*'''LRRK2''' or leucine-rich repeat Chk2 or dardarin
**[[6xr4]] – hLRRK2 – Cryo EM
**[[7lht]], [[7lhw]], [[7li4]] – hLRRK2 + ATP + GDP – Cryo EM
**[[7li3]] – hLRRK2 (mutant) + ATP + GDP – Cryo EM
**[[6oje]], [[7thy]] – hLRRK2 GTPase domain 1329-1520
**[[6ojf]] – hLRRK2 GTPase domain (mutant)
**[[6dlo]], [[6dlp]] – hLRRK2 WD40 domain
**[[7thz]] – hLRRK2 1330-1527 + GDP
**[[6vno]], [[6vp6]], [[6vp7]] – hLRRK2 C terminal 1330-2527 – Cryo EM
**[[6vp8]] – hLRRK2 C terminal 1330-2527 + COR domain 1670-1950 + WD40 domain 2140-2489 – Cryo EM
**[[6s6q]] – AtLRRK2 ectodomain + protein casparian strip peptide
*'''Pim'''
*Pim1 catalytic domain residues 14-313
**[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain
**[[1yxs]] – hPim1 catalytic domain (mutant)
**[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP
**[[1yxu]] – hPim1 catalytic domain + AMP
**[[1yxv]], [[5ipj]] – hPim1 catalytic domain + quinoline derivative
**[[1yxx]] – hPim1 catalytic domain + indole derivative
**[[2bzh]], [[2bzi]], [[2bzj]] – hPim1 catalytic domain (mutant) + organometallic ligand
**[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3c4e]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umw]], [[3umx]], [[4enx]], [[4eny]], [[4k1b]], [[4k18]], [[4k0y]], [[4iaa]], [[4i41]], [[4ll5]], [[4lm5]], [[4lmu]], [[4mta]], [[4med]], [[4mbl]], [[4mbi]], [[4n6y]], [[4n6z]], [[4n70]], [[4xh6]], [[5iis]], [[5kgd]], [[5kge]], [[5kgg]], [[5kgi]], [[5kgk]], [[5kzi]], [[5vua]], [[5vub]], [[5vuc]], [[6mt0]], [[6vrv]], [[7oov]], [[7oow]], [[7oox]], [[7xsv]] – hPim1 catalytic domain + inhibitor
**[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor
*Pim1 kinase domain residues 92-404
**[[4jx3]] – hPim1 kinase domain
**[[3uix]], [[5c1q]] – hPim1 kinase domain residues 120-404 + quinoline derivative
**[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate
**[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand
**[[1xws]], [[4alu]], [[4alv]], [[4alw]], [[4as0]], [[4bzn]], [[4bzo]], [[4dtk]], [[4jx7]], [[4rbl]], [[4rc2]], [[4rc3]], [[4rc4]], [[4ty1]], [[4wrs]], [[4wsy]], [[4wt6]], [[4xhk]], [[5dgz]], [[5dhj]], [[5dia]], [[5dwr]], [[5eol]], [[5kcx]], [[5o11]], [[5o12]], [[5o13]], [[5tel]], [[5tex]], [[5toe]], [[5v80]], [[5v82]]. [[6bsk]], [[6kzi]], [[6l11]], [[6l12]], [[6l13]], [[6l14]], [[6l15]], [[6l16]], [[6l17]], [[6no8]], [[6no9]], [[6vru]], [[6ykd]], [[7zun]] – hPim1 kinase domain + inhibitor
**[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor
*Pim1 full length
**[[4rpv]], [[5tur]] - hPim1 + inhibitor
*Pim1 complex with consensus peptide (pimtide)
**[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6qxk]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]] – hPim1 kinase domain + inhibitor + consensus peptide
**[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide
**[[2c3i]], [[5ndt]], [[5n5m]], [[5n5l]], [[5n52]], [[5n51]], [[5n50]], [[5n4z]], [[5n4y]], [[5n4x]], [[5n4v]], [[5n4u]], [[5n4r]], [[5n4o]], [[5n4n]], [[5mzl]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide
**[[4gw8]], [[7qb2]], [[7qfm]], [[7z6u]], [[8afr]] – hPim1 catalytic domain (mutant) + inhibitor + pimtide
**[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide
**[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide
*Pim1 containing phosphorylated Ser 261
**[[1yhs]] – hPim1 kinase domain + PSer + staurosporine
**[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor
**[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor
**[[1yi4]] – hPim1 kinase domain + PSer + adenosine
*Pim2
**[[4x7q]] – hPim2 catalytic domain + inhibitor
**[[2iwi]] – hPim2 catalytic domain + Ru ligand
*'''Rip or receptor-interacting Chk; Domains – catalytic 1-294; Amyloid fibril 418-518; Death 561-671'''
**[[6ac5]] – hRip1 death domain
**[[6r5f]], [[6nw2]], [[6c4d]], [[6c3e]], [[5tx5]], [[7fcz]], [[7fd0]], [[7ydx]] – hRip1 catalytic domain + inhibitor
**[[6rln]], [[6ocq]], [[6nyh]], [[6hho]] – hRip1 catalytic domain (mutant) + inhibitor
**[[6ggs]] – hRip2 – Cryo EM
**[[5yrn]] – hRip2 CARD domain 434-540 – Cryo EM
**[[6szj]], [[6sze]], [[6s1f]], [[6rna]], [[6rn8]], [[6hmx]], [[6fu5]], [[6es0]], [[5w5o]], [[5w5j]] – hRip2 catalytic domain + inhibitor
**[[6ul8]] – hRip2 catalytic domain (mutant) + inhibitor
**[[8aza]] – hRip2 catalytic domain + XiaP Bir2 domain – Cryo EM
**[[7mx3]] – hRip3 catalytic domain (mutant) + inhibitor
**[[7mon]] – hRip3 catalytic domain (mutant) + MLKL
**[[7dac]] – hRip3 amyloid fibril - NMR
**[[7da4]] – hRip3 amyloid fibril – Cryo EM
**[[6oko]] – mRip3 catalytic domain + inhibitor
**[[6jpd]] – mRip3 residues 409-486 - NMR
**[[5wnm]], [[5wnj]] – mRip4 catalytic domain (mutant) + drug
**[[5wnl]] – mRip4 catalytic domain (mutant) + staurosporine
**[[5wnk]] – mRip4 catalytic domain (mutant) + inhibitor
**[[5wni]] – mRip4 catalytic domain (mutant) + ATP
**[[6gwm]] – rRip2 caspase recruitment domain 433-539
*'''Ulk'''
**[[6qas]] – hChk Ulk1 + inhibitor
**[[5ci7]], [[6mnh]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[8soi]], [[8sqz]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein
**[[8srm]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein – Cryo EM
**[[8srq]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein + PI3K – Cryo EM
**[[6qav]], [[6qau]], [[6qat]], [[6yid]] – hChk Ulk2 + inhibitor
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[6fdz]], [[6fdy]] – hChk Ulk3 + leukemia drug
**[[6tsz]] – hChk Ulk4 pseudfokinase domain + ATPgS
**[[6u5l]] – hChk Ulk4 (mutant) + inhibitor
*'''Hipa''' and '''Hipb'''
**[[3tpd]], [[3tpe]] – EcChk Hipa – ''Escherichia coli''
**[[3tpb]], [[3dnt]], [[3dnu]] – EcChk Hipa (mutant)
**[[4pu7]], [[4pu8]] – SoChk Hipb - ''Shewanella oneidensis''
**[[3tpt]] – EcChk Hipa (mutant) + ADP
**[[3fbr]] – EcChk Hipa (mutant) + AMPPNP + peptide
**[[3tpv]] – EcChk Hipa + ADP
**[[2wiu]] – EcChk Hipa + Hipb
**[[4yg7]], [[5k98]], [[3hzi]], [[3dnv]] – EcChk Hipa + Hipb + DNA
**[[4yg1]], [[4z58]], [[4z59]], [[4z5c]], [[4z5d]] – EcChk Hipb + DNA
**[[4z5h]] – EcChk Hipb (mutant) + DNA
**[[4pu3]], [[4pu4]] – SoChk Hipa + Hipb + DNA - ''Shewanella oneidensis''
**[[4pu5]] – SoChk Hipa + AMPPNP
*'''Chk Smg'''
**[[6l53]] – hChk Smg1 – Cryo EM
**[[7pw6]] – hChk Smg1 + inhibitor – Cryo EM
**[[7pw7]] – hChk Smg1 + Smg9 + inhibitor – Cryo EM
**[[7pw9]] – hChk Smg1 + Smg9 + AMPPNP + ATP – Cryo EM
**[[6l54]], [[6syt]] – hChk Smg1 + Smg8 + Smg9 – Cryo EM
**[[7pw4]], [[7pw5]] – hChk Smg1 + Smg8 + Smg9 + inhibitor – Cryo EM
**[[7pw8]] – hChk Smg1 + Smg8 + Smg9 + AMPPNP – Cryo EM
**[[6z3r]] – hChk Smg1 + Smg8 + Smg9 + regulator of nonsense transcripts – Cryo EM
**[[2hwy]] – hChk Smg5 PIN domain
**[[2hww]], [[2hwx]] – hChk Smg6 PIN domain (mutant)
**[[4um2]] – hChk Smg6 TPR domain
**[[1ya0]] – hChk Smg7 N terminal
*'''Chk Vprbp or DCAF1'''
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain 1039-1401 (mutant)
**[[7sse]], [[7ufv]], [[8f8e]], [[8og5]], [[8og6]], [[8og7]], [[8og8]], [[8og9]], [[8oga]], [[8ogb]], [[8ogc]], [[8oo5]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) + inhibitor
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[5aja]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
*'''Other Chk'''
**[[1wak]] – hChk Sprk1
**[[3dak]] – hChk Osr1 kinase domain
**[[7okw]] – hChk Osr1 C-terminal
**[[4aw2]] – hChk Mrckα kinase domain
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain (mutant)
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[1uf0]] – hChk Dcamkl1 DCX domain – NMR
**[[1u5q]] – rChk Tao2 kinase domain
**[[2cos]] – mChk Lats2 – NMR
**[[1xte]], [[1xtn]], [[6edx]] – mChk Sgk3 PX domain
**[[4yom]] – mChk Brsk2
**[[4ynz]] – mChk Brsk1 N terminal domain
**[[5iri]] – mChk Brsk1 residues 592-719
**[[5oat]], [[7mp8]] – rfbChk Pink1– red flour beetle
**[[7t3x]] – Chk Pink1 (mutant) – louse
**[[4f0g]] – smChk Roco4 kinase domain – slime mold
**[[5tos]] – AtChk Bik1
**[[1q8z]], [[1zyc]] – yChk
**[[1how]], [[1zxe]], [[1zy4]] – yChk (mutant)
**[[1ow5]], [[1x9x]] – yChk Ste11 SAM domain – NMR
**[[2kio]], [[2kit]], [[1w1n]] – yChk Tor1 FATC domain – NMR
**[[3gre]] – yChk Vps15 WD repeat domain
**[[3osm]], [[3ost]] - yChk Kcc4 kinase domain
**[[5yyx]] – yChk Mek1 FHA domain
**[[6jxc]], [[6jxa]] – yChk Tel1 – Cryo EM
**[[6u69]] – CaChk Yck2 – ''Candida albicans''
**[[6sl1]], [[6sl0]], [[6skz]], [[6sky]] – Chk Tel1 – ''Chaetonium thermophilum'' – Cryo EM
**[[6ra0]] – CeChk Dkf1 – ''Chaenorhabditis elegans''
**[[7z6e]] – CeChk Mrck1 regulatory domain
**[[6tlb]] – Chk – ''Plasmodium falciparum''
*Other Chk complexes
**[[1wbp]], [[7dd1]] – hChk Sprk1 + peptide
**[[3beg]] – hChk Srpk1 + splicing factor SF2
**[[3hdm]], [[3hdn]], [[7pue]] – hChk Sgk1 (mutant) + inhibitor
**[[2r5t]] – hChk Sgk3 + AMPPNP
**[[4yff]], [[4yfi]], [[6b5j]], [[7mgj]], [[7mgk]] – hChk Tnni3k + inhibitor
**[[2v3s]] – hChk Osr1 + hChk Wnk4 peptide
**[[2vwi]] – hChk Osr1 kinase domain + ANP
**[[7que]], [[7quf]] – hChk Drak1 kinase domain + inhibitor
**[[4crs]] – hChk N2 kinase domain + ATPγS
**[[3tku]], [[4ual]], [[3qfv]], [[5ote]], [[5otf]] – hChk Mrckβ + inhibitor
**[[4uak]] – hChk Mrckβ + ADP
**[[5aja]], [[4z8l]], [[4cc9]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
**[[5jk7]] – hChk Vprbp WD repeat domain + VPX + DDB1 + UDG
**[[3wa0]], [[4p7i]] – hChk Vprbp residues 1417-1506 + merlin
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[5ci7]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[5b5w]], [[5b6b]], [[5brk]] – hChk Lats1 residues 622-704 + MOB1
**[[5yz0]] – hChk Atr + Atr-interacting protein – Cryo EM
**[[6bdn]] – hChk Tao3 kinase domain + ADP
**[[5yh3]] – hChk Fam20C 141-578 + pseudokinase Fam20A
**[[2gcd]] – rChk Tao2 kinase domain + staurosporine
**[[1u5r]] – rChk Tao2 kinase domain + ATP
**[[5yj9]], [[7mp9]] – rfbChk Pink1 kinase domain + AMPPNP
**[[6bn1]] – DmChk Hippo SARAH domain + Shar-Pei
**[[3hgk]] – Chk Pto + effector protein AVRPTOB – Currant tomato
**[[3p86]], [[3ppz]] - AtChk Ctr1 + staurosporine
**[[4f0f]] – smChk Roco4 kinase domain + APPCP
**[[4f1m]], [[4f1o]] – smChk Roco4 kinase domain (mutant) + APPCP
**[[4f1t]], [[4yzm]], [[4yzn]] – smChk Roco4 kinase domain + inhibitor
**[[5fvm]] - Tor2 + LST8 - ''Kluyveromyces marxianus''
**[[5kc2]] - yVps15 + Vps34 - Cryo EM
**[[5dfz]] - yVps15 + Vps34 + Vps30 + VPSAP28 + VPSAP30 - Cryo EM
**[[1q8y]], [[1q97]], [[1q99]], [[1zyd]] – yChk + nucleotide
**[[1zy5]] – yChk (mutant) + nucleotide
**[[2jd5]] – yChk + NPL-3P
**[[4lqs]], [[4lqq]], [[4lqp]] – yChk Cbk1 residues 251-756 + Cbk1 activator Mob2
**[[6emk]] – yChk Tor2 + LST8 + TSC11 + AVO1 + AVO2 – Cryo EM
**[[6s8f]] – yChk Tel1 + AMPPNP – Cryo EM
**[[5yyz]] – yChk Mek1 FHA domain + Hop1
**[[5x6o]], [[6z3a]], [[7wzr]], [[7wzw]]– yChk Mec1 + LCD1 – Cryo EM
**[[6z2w]], [[6z2x]] – yChk Mec1 (mutant) + LCD1 – Cryo EM
**[[7kue]] – yChk Kin28 in TFIIK complex – Cryo EM
**[[6u6a]] – CaChk Yck2 + inhibitor
**[[5fvm]] – Chk Tor2 + LST8 – ''Kluyveromyces maximanus''
*Serine/threonine protein kinase Rad53 see [[Rad53]]
*Serine/threonine protein kinase Gsk3B see [[Glycogen synthase kinase 3]]
}}
[[Category:Topic Page]]

Serine/threonine protein kinase 3D structures

2026-08-19T07:25:40Z

Michal Harel:

==3D structures of serine/threonine protein kinase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Chk1'''; domains - kinase 1-289; KA1 393-492
**[[1ia8]] – hChk1 kinase domain – human
**[[5w12]] – hChk1 KA1 domain
**[[1zlt]] – hChk1 kinase domain + hymenaldisine
**[[1nvq]], [[1nvr]] – hChk1 kinase domain + peptide + saurosporine
**[[1nvs]], [[1zys]], [[7ako]] - hChk1 kinase domain + peptide + inhibitor
**[[7akm]] - hChk1 kinase domain + ATP
**[[2ayp]], [[2br1]], [[2brb]], [[2brg]], [[2brh]], [[2brm]], [[2brn]], [[2bro]], [[2c3j]], [[2c3k]], [[2c3l]], [[2cgu]], [[2cgv]], [[2cgw]], [[2cgx]], [[2e9n]], [[2e9o]], [[2e9p]], [[2e9u]], [[2e9v]], [[2gdo]], [[2ghg]], [[2hog]], [[2hxl]], [[2hxq]], [[2hy0]], [[2qhm]], [[2qhn]], [[2r0u]], [[3f9n]], [[2wmq]], [[2wmr]], [[2wms]], [[2wmt]], [[2wmu]], [[2wmv]], [[2wmw]], [[2wmx]], [[2xey]], [[2xf0]], [[2xez]], [[2x8d]], [[2x8e]], [[2x8i]], [[2ydi]], [[2ydj]], [[2ydk]], [[2yer]], [[2yex]], [[2ym3]], [[2ym4]], [[2ym5]], [[2ym6]], [[2ym7]], [[2ym8]], [[2ywp]], [[3jvr]], [[3jvs]], [[3nlb]], [[3ot3]], [[3ot8]], [[3pa3]], [[3pa4]], [[3pa5]], [[3tkh]], [[3tki]], [[3u9n]], [[4fsm]], [[4fsn]], [[4fsq]], [[4fsr]], [[4fst]], [[4fsu]], [[4fsw]], [[4fsy]], [[4fsz]], [[4ft0]], [[4ft3]], [[4ft5]], [[4ft7]], [[4ft9]], [[4fta]], [[4ftc]], [[4fti]], [[4ftj]], [[4ftk]], [[4ftl]], [[4ftm]], [[4ftn]], [[4fto]], [[4ftq]], [[4ftr]], [[4ftt]], [[4ftu]], [[4gh2]], [[4hyh]], [[4hyi]], [[4jik]], [[4qye]], [[4qyf]], [[4qyg]], [[4qyh]], [[4rvk]], [[4rvl]], [[4rvm]], [[5dls]], [[5f4n]], [[5fcf]], [[5fck]], [[6fc8]], [[6fcf]], [[6fck]], [[7bko]], [[8e80]], [[8e81]] - hChk1 kinase domain + inhibitor 
**[[5oot]], [[5op2]], [[5op4]], [[5op5]], [[5op7]], [[5opb]], [[5opr]], [[5ops]], [[5opu]], [[5opv]], [[5oq5]], [[5oq6]], [[5oq7]], [[5oq8]], [[7bjd]], [[7bjh]], [[7bjj]], [[7bjm]], [[7bjo]], [[7bjr]], [[7bjx]], [[7bk1]], [[7bk2]], [[7bk3]], [[7mck]], [[7suf]], [[7sug]], [[7suh]], [[7sui]], [[7suj]], [[8siv]], [[8siw]], [[8six]] - hChk1 kinase domain (mutant) + inhibitor
**[[5oop]] - hChk1 kinase domain (mutant) + AMPPNP
**[[5oor]] - hChk1 kinase domain (mutant) + staurosporine
**[[7bkn]] - hChk1 kinase domain + adenine
**[[7bje]] - hChk1 kinase domain (mutant) + adenine
**[[2jqi]] – yChk1 – yeast
*'''Chk2 (Checkpoint kinase)'''
**[[1gxc]] – hChk2 phosphothreonine-binding domain + phosphopeptide
**[[2cn5]] – hChk2 kinase domain + ADP
**[[2cn8]] – hChk2 kinase domain + inhibitor
**[[2cn8]], [[2uv2]], [[2w0j]], [[2w7x]], [[2wtc]], [[2wtd]], [[2wti]], [[2wtj]], [[2xbj]], [[2xk9]], [[2xm8]], [[2xm9]], [[2ycf]], [[2ycq]], [[2ycr]], [[2ycs]], [[2yiq]], [[2yir]], [[2yit]], [[4a9r]], [[4a9s]], [[4a9t]], [[4bda]], [[4bdb]], [[4bdc]], [[4bdd]], [[4bde]], [[4bdf]], [[4bdg]], [[4bdh]], [[4bdi]], [[4bdj]], [[4bdk]] - hChk2 kinase domain + inhibitor
**[[3i6u]], [[3i6w]] – hChk2 residues 84-502 (mutant)
*'''Chk3 (Mst2)'''; domains - kinase 13-313; SARAH 436-484
**[[3wws]], [[4hkd]], [[4l0n]], [[4oh9]] – hChk3 SARAH domain 
**[[4lg4]] – hChk3 kinase domain
**[[4lgd]] – hChk3 kinase domain + RASSF5 SARAH domain
**[[6ao5]] – hChk3 kinase+SARAH domains (mutant) + SAV1 SARAH domain
**[[5dh3]], [[8a66]] – hChk3 kinase domain + inhibitor
*'''Chk4 (Mst1)''' ; Domains – kinase 1-311; SARAH 432-480
**[[3com]] – hChk4 kinase domain
**[[6yat]], [[8a5j]]– hChk4 kinase domain + inhibitor
**[[4nr2]] – hChk4 SARAH domain
**[[2jo8]] – hChk4 SARAH domain - NMR
**[[4oh8]] – hChk4 SARAH domain + Ras association domain-containing protein
*'''Chk5 (Aurora kinase b)'''
**[[4af3]] – hChk5 + inhibitor
*'''Chk6 or Chk15 or Aurora kinase A'''
**[[1mq4]], [[1muo]], [[4j8n]], [[4o0s]], [[6cpe]] – hChk6 kinase domain 
**[[4bn1]], [[4o0w]], [[4o0u]] – hChk6 kinase domain (mutant)
**[[5dnr]], [[5drd]], [[5dt3]] – hChk6 kinase domain + ATP
**[[5drd]] – hChk6 kinase domain + ATP
**[[1ol6]] – hChk6 kinase domain (mutant) + ATP
**[[2wqe]] – hChk6 kinase domain (mutant) + ADP
**[[5odt]] – hChk6 kinase domain (mutant) + ADP + TACC3
**[[2c6d]] – hChk6 kinase domain (mutant) + ADPNP
**[[2dwb]] – hChk6 kinase domain + AMPPNP
**[[6cpf]] – hChk6 kinase domain + AMPPCP
**[[5g15]] – hChk6 kinase domain + AMPPNP + monobody
**[[6cpg]], [[8ssp]] – hChk6 kinase domain + inhibitor + monobody
**[[2j4z]], [[2j50]], [[2np8]], [[2x81]], [[2x6d]], [[2x6e]], [[3efw]], [[3myg]], [[3vap]], [[3w10]], [[3w16]], [[3w18]], [[3w2c]], [[4b0g]], [[4byi]], [[4byj]], [[4j8m]], [[4jai]], [[4jaj]], [[4uyn]], [[4uzd]], [[4uzh]], [[4zs0]], [[4ztq]], [[4ztr]], [[4zts]], [[5aad]], [[5aae]], [[5aag]], [[5dpv]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5obr]], [[5one]], [[5zan]], [[6c2r]], [[6c2t]], [[6gra]], [[6z4y]], [[7ayh]], [[7ayi]], [[7fic]], [[7o2v]], [[8jmx]] – hChk6 kinase domain + inhibitor 
**[[2bmc]], [[2c6e]], [[2wtw]], [[2xne]], [[2xng]], [[2xru]], [[3coh]], [[3fdn]], [[3h0y]], [[3h0z]], [[3h10]], [[3lau]], [[3k5u]], [[3m11]], [[3nrm]], [[3p9j]], [[3r21]], [[3r22]], [[3qbn]], [[3unz]], [[3uo4]], [[3uo5]], [[3uo6]], [[3uod]], [[3uoh]], [[3uoj]], [[3uok]], [[3uol]], [[3up2]], [[3up7]], [[4dea]], [[4deb]], [[4ded]], [[4dee]], [[4dhf]], [[4jbo]], [[4jbp]], [[4jbq]], [[4prj]], [[5aad]], [[5aae]], [[5aaf]], [[5aag]], [[5dpv]], [[6hjj]], [[6hjk]] – hChk6 kinase domain (mutant) + inhibitor 
**[[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[5dos]], [[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5dn3]], [[5dos]], [[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[6c83]] – hChk6 kinase domain + AMPPCP + nanobody
**[[8sso]] – hChk6 kinase domain + drug + monobody
**[[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5g1x]], [[7ztl]] – hChk6 kinase domain (mutant) + N-Myc
**[[8guw]] – hChk6 kinase domain/activator peptide
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + Targeting protein for XKLP2
**[[3daj]], [[3d14]], [[3dj5]], [[3dj6]], [[3dj7]], [[3d15]], [[3d2i]], [[3d2k]] – Chk6 kinase domain (mutant) + inhibitor - mouse
*Chk6 with phosphorylated Thr 287, Thr288
**[[1ol5]], [[1ol7]] – hChk6 kinase domain + PThr + ADP
**[[5dnr]], [[5dt3]] – hChk6 kinase domain + PThr + ATP
**[[2w1c]], [[2w1d]], [[2w1e]], [[2w1f]], [[2w1g]], [[5dn3]] – hChk6 kinase domain + PThr + inhibitor
**[[2wtv]], [[5orl]], [[5orn]], [[5oro]], [[5orp]], [[5orr]], [[5ors]], [[5ort]], [[5orv]], [[5orw]], [[5orx]], [[5ory]], [[5orz]], [[5os0]], [[5os1]], [[5os2]], [[5os3]], [[5os4]], [[5os5]], [[5os6]], [[5osd]], [[5ose]], [[5osf]] – hChk6 kinase domain (mutant) + PThr + inhibitor
**[[3e5a]], [[3ha6]] – hChk6 kinase domain + PThr + inhibitor + targeting protein for XKLP2
**[[5g1x]] – hChk6 kinase domain (mutant) + PThr + N-Myc
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + PThr + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + PThr + TPX2
**[[6r4d]], [[6r4c]], [[6r4b]], [[6r4a]] – hChk6 kinase domain + PThr + inhibitor + ADP
**[[6i2u]] – hChk6 kinase domain (mutant) + PThr + inhibitor + ADP
**[[6r49]] – hChk6 kinase domain (mutant) + PThr + CoA
*'''Chk10 (lymphocyte-oriented kinase)''' or LOK or STK10
**[[7qgp]] – hChk10
**[[2j7t]], [[4aot]], [[4equ]], [[4usd]], [[4use]], [[5ajq]], [[5owq]], [[5owr]], [[6eim]], [[6gtt]], [[6i2y]], [[6hxf]] – hChk10 kinase domain + inhibitor
**[[4bc6]], [[6i2y]] – hChk10 + drug
*'''Chk11'''
**[[2wtk]] – hChk11 (mutant) + calcium-binding protein
*'''Chk12-A (Aurora kinase b-a or Aurora B kinase)'''
**[[2vgo]], [[2vgp]], [[2vrx]], [[3ztx]], [[4c2v]], [[5eyk]] – fChk12-A + inner centromere protein A peptide + inhibitor - frog
**[[4c2w]] – fChk12-A + inner centromere protein A peptide + AMPPNP
**[[4b8l]], [[4b8m]], [[5k3y]] – fChk12-A (mutant) + inner centromere protein A peptide + inhibitor
*'''Chk13 (Polo-like kinase Plk)'''
*Plk1 Polo-box domain (Pbd) 371-594''
**[[1q4o]], [[2ogq]], [[3hih]], [[3p2w]], [[4h5x]], [[6n46]] – hPlk1 Pbd
*Plk1 Pbd complex with polypeptide
**[[1umw]], [[2ojx]], [[3bzi]], [[3c5l]], [[3rq7]], [[4dfw]], [[4whl]], [[4whk]], [[4whh]], [[4rcp]], [[4o6w]], [[4o56]], [[5dms]], [[5dmv]], [[5dnj]] , [[7mso]], [[7mx1]] – hPlk1 + peptide
**[[3hik]], [[3fvh]], [[3p2z]], [[3p34]], [[3p35]], [[3p36]], [[3p37]], [[3q1i]], [[4e67]], [[4e9c]], [[4e9d]], [[4hab]], [[4hy2]], [[4o9w]], [[4x9r]], [[4x9v]], [[4x9w]], [[5j19]], [[6gy2]] – hPlk1 + phosphopeptide
**[[1q4k]] – hPlk1 (mutant) + phosphopeptide
**[[2v5q]] – hPlk1 + design ankyrin repeat protein
**[[4lkl]] – hChk Plk1 + PL-55
**[[4lkm]] – hChk Plk1 + PL-74
**[[6ax4]] – hChk Plk1 + histidine cyclized macrocycle
**[[5x3s]] – mPlk1 + phosphopeptide
**[[8joq]], [[8joy]] – hPlk1 Pbd + hpv peptide
*Plk1 Pbd complex with small molecule inhibitor
**[[4h71]], [[4hco]], [[5ta6]], [[5ta8]], [[8bjt]], [[8crc]] – hPlk1 + inhibitor
**[[2rku]] – hPlk1 (mutant) + inhibitor
**[[3db6]], [[3db8]], [[3dbc]], [[3dbd]], [[3dbe]], [[3dbf]] – zfPlk1 (mutant) + inhibitor – zebra fish
*Plk1 catalytic domain 36-345
**[[2owb]] – hPlk1 catalytic domain (mutant)
**[[2ou7]] – hPlk1 catalytic domain (mutant) + AM
**[[3kb7]], [[2yac]], [[3thb]], [[4a4l]], [[4a4o]] – hPlk1 catalytic domain + inhibitor
**[[3fc2]] – hPlk1 catalytic domain (mutant) + inhibitor
**[[4j52]], [[4j53]] – hChk Plk1 (mutant) + inhibitor
**[[3d5x]] – zfPlk1 catalytic domain (mutant) + wortmannin
**[[3d5w]] – zfPlk1 catalytic domain + ADP
*'''Plk2'''
**[[4i5m]], [[4i5p]], [[4i6b]], [[4i6f]], [[4i6h]] – hChk Plk2 kinase domain (mutant) + inhibitor
**[[4xb0]], [[4rs6]] – hChk Plk2 Pbd
*'''Plk3'''
**[[4b6l]], [[4i6b]] – hChk Plk3 kinase domain + inhibitor
*'''Plk4'''; Domains – kinase 2-275; Pbd 580-808; Pb3 884-970
**[[3cok]] – hChk Plk4 kinase domain
**[[4n9j]] – hChk Plk4 Pbd domain
**[[4n7z]], [[4n7v]] – hChk Plk4 Pbd domain + centrosomal protein
**[[6w38]], [[6w3i]] – hChk Plk4 Pbd domain + Fam46C
**[[6w3j]] – hChk Plk4 Pbd domain + Fam46C + CEP92 peptide
**[[4jxf]], [[4yur]] – hChk Plk4 kinase domain + inhibitor
**[[5lhy]] – hChk Plk4 Pb3 domain
**[[4yyp]], [[5lhz]] – hChk Plk4 Pb3 domain + Scl-interrupting locus protein
**[[4nk7]], [[4g7n]], [[5lhx]], [[7rl3]] – DmChk Plk4 Pbd domain – ''Drosophila melanogaster''
*'''Chk16'''
**[[2buj]] – hChk16 (mutant) + staurosporin
*'''Chk17B''' or DRAK2 or STK17B
**[[3lm0]] – hChk17B
**[[6qf4]], [[7q7c]], [[7q7d]] – hChk17B + ADP
**[[7q7e]] – hChk17B + ATP
**[[3lm5]] – hChk17B + quercetin
**[[6y6f]], [[6y6h]], [[6zjf]] – hChk17B + pyrimidine derivative
**[[7akg]] – hChk17B + drug
*'''Chk19''' or STK19
**[[7xrb]] – hChk19
*'''Chk24 (Mst3)''' or STK24
**[[3a7f]], [[3a7g]], [[3a7h]], [[3a7i]], [[3a7j]], [[3ckw]] – hChk24 kinase domain
**[[4w8e]], [[4w8d]], [[4u8z]], [[4qmm]], [[4qmn]], [[4qmo]], [[4qmp]], [[4qmq]], [[4qms]], [[4qmt]], [[4qmu]], [[4qmv]], [[4qmw]], [[4qmx]], [[4qmy]], [[4qmz]], [[4qna]], [[4qo9]], [[4u8z]], [[7b30]], [[7b31]], [[7b32]], [[7b33]], [[7b34]], [[7b35]], [[8bzi]], [[8bzj]], [[8qlr]], [[8qls]], [[8qlt]] – hChk Mst3 + inhibitor
**[[8qlq]] – hChk Mst3 + macrocyclic inhibitor
**[[3ckx]] – hChk24 kinase domain + staurosporin
**[[3zhp]] – hChk24 kinase domain + calcium-binding protein
**[[4o27]] – hChk24 kinase domain (mutant) + calcium-binding protein
**[[4qml]] – hChk Mst3 kinase domain + AMPPNP
*'''Chk25 or STK25'''
**[[2xik]] – hChk25 kinase domain
**[[7z4v]] – hChk25 kinase domain + inhibitor
**[[3w8h]] – hChk25 regulatory domain + programmed cell death protein 10
**[[4nzw]] – hChk25 kinase domain (mutant) + calcium-binding protein
*'''Chk26 (Mst4)'''
**[[3ggf]], [[7b36]] – hChk Mst4 + inhibitor
**[[4geh]], [[3w8i]] - hChk Mst4 dimerization domain + programmed cell death protein 10
**[[4fza]], [[4fzd]], [[4fzf]] – hChk Mst4 (mutant) + calcium-binding protein
*'''Chk32'''
**[[4fr4]] – hChk32A
*'''Chk38'''
**[[6bxi]] – hChk38 kinase domain
*'''Chk39''' or SPAK
**[[7o86]] – hChk39 C-terminal
**[[5d9h]] – mChk39 residues 63-403 + ATP
**[[5dbx]] – mChk39 residues 63-403 (mutant) + AMPPNP
*'''Chk40'''
**[[5l2q]] – hChk40 kinase homology domain
*'''Dclk1'''
**[[6kyq]] – hChk Dclk1 kinase domain
**[[6kyr]] – hChk Dclk1 kinase domain (mutant)
**[[5jzj]] – hChk Dclk1 kinase domain + AMPPN
**[[5jzn]], [[7kx6]], [[7kxw]] – hChk Dclk1 kinase domain + inhibitor
**[[7f3g]] – hChk Dclk1 kinase domain + drug
**[[7kx8]] – hChk Dclk1 C-terminal + inhibitor
*'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123; kinase 144-480
**[[1unp]], [[1unr]] – hRac-α hChk pleckstrin homology domain
**[[2uzr]], [[2uzs]], [[7myx]] – hRac-α hChk pleckstrin homology domain (mutant)
**[[1h10]], [[1unq]], [[2uvm]] – hRac-α hChk pleckstrin homology domain + inositol tetrakisphosphate
**[[3o96]], [[4ejn]], [[6s9w]], [[6s9x]], [[6hhj]], [[6hhi]], [[6hhh]], [[6hhg]], [[6hhf]] - hRac-α hChk + inhibitor
**[[5kcv]], [[7nh4]], [[7nh5]] - hRac-α hChk (mutant) + inhibitor
**[[4gv1]], [[4ekl]] - hRac-α hChk kinase domain + inhibitor
**[[3qkm]], [[6ccy]] - hRac-α hChk kinase domain (mutant) + inhibitor
**[[6buu]] - hRac-α hChk kinase domain + bisubstrate peptide
**[[4ekk]] - hRac-α hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[6npz]] - hRac-α hChk kinase domain + peptide + inhibitor
**[[3ow4]], [[3qkk]], [[3qkl]], [[6buu]] - hRac-α hChk kinase domain (mutant) + peptide + inhibitor
**[[7apj]] - hRac-α hChk + nanobody
*'''Rac-β hChk (AKT2)'''
**[[1gzk]], [[1gzn]], [[1gzo]], [[1mrv]], [[1mry]] – hRac-β hChk kinase domain
**[[1p6s]] - hRac-β hChk pleckstrin homology domain - NMR
**[[1o6k]] - hRac-β hChk kinase domain + GSK3 peptide + AMPPNP
**[[2jdo]], [[2jdr]], [[2uw9]], [[2x39]], [[3cqu]], [[3cqw]] - hRac-β hChk kinase domain + GSK3 peptide + inhibitor
**[[3e87]], [[3e88]], [[3e8d]] - Rac-β hChk kinase domain (mutant) + GSK3 peptide + inhibitor<br /
**[[1o6l]] - hRac-β hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[3d0e]], [[8q61]] - hRac-β hChk kinase domain (mutant) + inhibitor
*'''Rac-γ hChk (ATK3)'''
**[[2x18]] – Rac-γ hChk PH domain
*'''A-Raf'''
**[[1wxm]] – hA-Raf RAS-binding domain 19-91 - NMR
**[[2mse]] – hA-Raf RAS-binding domain + APOA-I + K-ras - NMR
*'''B-Raf'''; domains - BRS 38-116; Ras-binding 153-237; kinase 445-723
**[[8dgs]], [[8dgt]] – hB-Raf in Ras/Raf complex – Cryo EM
**[[7z37]], [[7z38]], [[7zr5]] – hB-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
**[[1uwh]], [[3c4c]], [[6v2u]], [[6xfp]], [[6xlo]], [[8f7o]], [[8f7p]] – hB-Raf kinase domain + anticancer drug
**[[1uwj]], [[6p3d]] – hB-Raf kinase domain (mutant) + anticancer drug
**[[2fb8]], [[3d4q]], [[3ii5]], [[3psd]], [[3skc]], [[3tv6]], [[4g9c]], [[4ksp]], [[4ksq]], [[3psb]], [[3ppj]], [[3ppk]], [[3prf]], [[3pri]], [[3tv4]], [[4dbn]], [[4e4x]], [[4mbj]], [[4ehe]], [[3q4c]], [[3q96]], [[3e26]], [[4h58]], [[4e26]], [[4fc0]], [[4pp7]], [[6cad]], [[7shv]] – hB-Raf kinase domain + pyrazole inhibitor
**[[4jvg]], [[4ehg]], [[4fk3]], [[3idp]], [[4g9r]], [[4wo5]], [[4mnf]], [[4r5y]], [[4rzv]], [[4rzw]], [[4xv1]], [[4xv2]], [[4xv3]], [[4xv9]], [[4yht]], [[5c9c]], [[5hi2]], [[5ita]], [[5jrq]], [[5jsm]], [[5jt2]], [[6nsq]], [[6p7d]], [[6uuo]] – hB-Raf kinase domain (mutant) + pyrazole inhibitor
**[[5csw]], [[5csx]], [[5ct7]], [[5fd2]], [[5hid]], [[5hie]], [[5val]], [[5vam]], [[6b8u]], [[6n0q]], [[6n0p]], [[7k0v]], [[7p3b]], [[7p3v]], [[8c7x]], [[8c7y]] - hB-Raf kinase domain + inhibitor
**[[6v34]] – hB-Raf kinase domain (mutant) + inhibitor
**[[4mne]] – hB-Raf kinase domain + MAPKK1
**[[8f7o]] – hB-Raf kinase domain + drug
**[[7m0u]] – hB-Raf kinase domain + AMPPNP + drug
**[[6u2h]] – hB-Raf kinase domain + 14-3-3 ζ/δ
**[[7mfe]] – hB-Raf + 14-3-3 ζ/δ – Cryo EM
**[[7mff]] – hB-Raf + 14-3-3 ζ/δ + inhibitor – Cryo EM
**[[7mfd]] – hB-Raf + 14-3-3 ζ/δ + MEK + inhibitor – Cryo EM
**[[6pp9]] – hB-Raf kinase domain + MEK1 + ANP
**[[7m0x]], [[7m0z]] – hB-Raf kinase domain + MEK1 + ANP + inhibitor
**[[7m0t]], [[7m0u]], [[7m0v]], [[7m0w]], [[7m0y]] – hB-Raf kinase domain + MEK1 + ANP + drug
**[[6u2g]] – hB-Raf kinase domain + MEK1 + AMPPCP
**[[5vr3]] – hB-Raf BRS domain
**[[7jhp]] – hB-Raf BRS domain + Hras
**[[6ntc]], [[6ntd]] – hB-Raf BRS domain (mutant) + Hras
**[[6xi7]] – hB-Raf 52-188 + Kras
**[[2l05]], [[5j17]], [[5j2r]] – hB-Raf RAS-binding domain - NMR
**[[3ny5]] – hB-Raf RAS-binding domain
**[[5j18]] – hB-Raf RAS-binding domain + inhibitor - NMR
**[[6pts]], [[6ptw]] – hB-Raf 56-187 + Kras + apolipoprotein + GMPPNP - NMR
**[[6uan]], [[6q0k]] – hB-Raf + 14-3-3 ζ – Cryo EM
**[[6nyb]] – hB-Raf + 14-3-3 ζ + MEK1 – Cryo EM
**[[6q0t]], [[6q0j]] – hB-Raf (mutant) + 14-3-3 ζ + MEK1 – Cryo EM
*'''c-Raf'''; Domains – RAS-binding (RBD) 55-132; Cys-rich 136-187 (CBD); kinase 323-618
**[[1rfa]], [[8jna]], [[8jof]], [[8jog]] – hc-Raf RBD - NMR
**[[1faq]], [[1far]] – hc-Raf cysteine-rich domain - NMR
**[[3omv]] – hc-Raf kinase domain
**[[1rrb]] – c-Raf RBD – NMR - rat
*c-Raf complex with protein
**[[8cpd]] – hc-Raf + 14-3-3 protein zeta – Cryo EM
**[[9mmp]] – hc-Raf + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[9mmr]] – hc-Raf (mutant) + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[1c1y]] – hc-Raf RBD + RAP1A
**[[3kuc]] – hc-Raf RBD (mutant) + RAP1A
**[[1gua]] – hc-Raf RBD + RAP1A + GPPNHP
**[[8jnb]] – hc-Raf RBD + ligand
**[[4g0n]], [[4g3x]] – hc-Raf RBD + GTPase Hras
**[[3kud]] – hc-Raf RBD (mutant) + GTPase Hras
**[[8epw]], [[8t74]] – hc-Raf RBD + GTPase K-ras
**[[8t75]], [[9ygs]] – hc-Raf RBD-CRD + GTPase K-ras + GMPPNP
**[[9ay7]], [[9aya]] – hc-Raf + MEK1
**[[9mmq]] – hc-Raf + MEK1 – Cryo EM
**[[9mms]] – hc-Raf (mutant) + MEK1 – Cryo EM
**[[9o0u]], [[9o0v]] – hc-Raf (mutant) + MEK1 + ANP + inhibitor– Cryo EM
**[[8u1l]] – hc-Raf + Hsp90 + CDC37 – Cryo EM
**[[8gae]], [[8gft]] – hc-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
*'''Snf1-related Chk'''
**[[3uc4]], [[3uc3]], [[3udb]], [[3zut]], [[3zuu]] – AtChk Srk2E kinase domain (mutant) – ''Arabidopsis thaliana''
**[[3ujg]] – AtChk Srk2E kinase domain (mutant) + protein phosphatase 2C
**[[5yks]] – hChk
*'''MAPK-interacting Chk''' or Mnk1 Mnk2
**[[2hw6]] – hMnk 1 catalytic domain
**[[2hw7]] – hMnk 1 catalytic domain + staurosporin
**[[5wvd]] – hMnk 1 catalytic domain + inhibitor
**[[2ac3]] – hMnk 2 catalytic domain
**[[2ac5]] – hMnk 2 catalytic domain (mutant)
**[[6cj5]], [[6cje]], [[6cjh]], [[6cjw]], [[6cjy]], [[6ck3]], [[6ck6]], [[6cki]] – hMnk 2 catalytic domain (mutant) + inhibitor
*'''hChk Pak''' or '''Chk N''' or '''PRK1'''; Domains - CRIB 74-109; Hr1B 122-199; catalytic 109-426; kinase 605-942
**[[1urf]] – hChk Pak-1 Hr1b domain - NMR
**[[4nkg]] – hChk Pak-1 Hr1b domain + SSPH1 LRR domain
**[[2rmk]] – hChk Pak-1 Hr1bb domain + Rac1 - NMR
**[[1f3m]] – hChk Pak-1 autoregulatory+kinase domains
**[[4otd]] - hChk Pak-1 kinase domain
**[[1yhv]], [[1yhw]], [[3q4z]], [[3q52]], [[3q53]] – hChk Pak-1 kinase domain (mutant)
**[[4o0r]], [[4o0t]], [[4zji]], [[4zjj]], [[4zlo]], [[4zy4]], [[4zy5]], [[4zy7]], [[5ime]], [[5kbq]], [[5kbr]], [[6b16]], [[7vto]] – hChk Pak-1 kinase domain + inhibitor
**[[4oti]], [[4oth]], [[4otg]] – hChk Pak-1 kinase domain + inhibitor
**[[4eqc]], [[4p90]], [[5dew]], [[5dey]], [[5dfp]] – hChk Pak-1 kinase domain (mutant) + inhibitor
**[[2hy8]] – hChk Pak-1 kinase domain + staurosporin
**[[2qme]] – hChk Pak-1 CRIB domain + RAC3
**[[3fxz]], [[3fy0]], [[4daw]] – hChk Pak-1 kinase domain (mutant) + Ru complex
**[[6fd3]] – hChk Pak-3 kinase domain (mutant)
**[[2j0i]], [[4fie]] – hChk Pak-4
**[[4fig]], [[4fij]], [[4l67]] – hChk Pak-4 kinase domain
**[[2cdz]] – hChk Pak-4 + purine derivative
**[[2ov2]] – hChk Pak-4 CRIB domain + RAC3
**[[2qon]], [[4fif]], [[4fih]], [[4fii]], [[4jdh]], [[4jdi]], [[4jdj]], [[4jdk]], [[6wlx]], [[6wly]] – hChk Pak-4 kinase domain + peptide
**[[4app]], [[4o0v]], [[4o0x]], [[4o0y]], [[4njd]], [[4xbu]], [[5bms]], [[5i0b]], [[5vee]], [[5vef]], [[5zjw]], [[5xvg]], [[5xvf]], [[5xva]], [[7cmb]], [[7cp3]], [[7cp4]] – hChk Pak-4 kinase domain + inhibitor
**[[2x4z]], [[2xh5]] – hChk Pak-4 kinase domain (mutant) + inhibitor
**[[5upl]], [[5upk]] – hChk Pak-4 kinase domain (mutant) + CDC42
**[[5ved]] – hChk Pak-4 kinase domain + staurosporine
**[[8ahi]] – hChk Pak-4 300-591 + inhibitor
**[[7s46]], [[7s48]] – hChk Pak-4 catalytic domain + integrin beta-5 peptide
**[[2c30]] – hChk Pak-6
**[[2odb]] – hChk Pak-6 CRIB domain + CDC42
**[[4ks8]] – hChk Pak-6 kinase domain + sunitinib
**[[4ks7]] – hChk Pak-6 kinase domain (mutant) + inhibitor
**[[2f57]] – hChk Pak-7
*'''Mycobacterium tuberculosis Chk Pkn'''
**[[4x3f]] - MtChk PknA – ''Mycobacterium tuberculosis''
**[[4ow8]] - MtChk PknA kinase domain
**[[3ori]], [[3ork]], [[3orl]], [[3orm]], [[3oro]], [[3orp]], [[3ort]] - MtChk PknB kinase domain (mutant)
**[[1o6y]] – MtChk PknB kinase domain
**[[6b2p]], [[6b2q]] – MtChk PknB kinase domain + inhibitor
**[[2kud]], [[2kue]], [[2kuf]], [[2kui]] – MtChk PknB pasta domains 2-3 - NMR
**[[3ouv]] – MtChk PknB pasta domain 3
**[[5e0y]] – MtChk PknB pasta domain 4
**[[5e10]] – MtChk PknB pasta domains 1-2
**[[5e0z]] – MtChk PknB pasta domains 3-4
**[[5e12]] – MtChk PknB pasta domains 2-4
**[[5u94]] - MtChk PknB kinase domain + inhibitor
**[[3f61]], [[3f69]] - MtChk PknB kinase domain (mutant) + inhibitor
**[[6i2p]] - MtChk PknB kinase domain (mutant) + GARA + peptide
**[[1rwi]], [[1rwl]] - MtChk PknD extracellular domain
**[[2h34]] – MtChk PknE catalytic domain
**[[7naa]] – MtChk PknF kinase domain + inhibitor
**[[4y12]] - MtChk PknG + ATP-gS
**[[4y0x]] - MtChk PknG + ADP
**[[7q52]] - MtChk PknG + inhibitor
**[[4esq]] - MtChk PknH extracellular domain
**[[5m06]], [[5xka]] - MtChk PknI kinase domain
**[[5m07]], [[5m08]], [[5m09]] - MtChk PknI kinase domain (mutant)
**[[5xlm]], [[5xll]] - MtChk PknI sensor domain
**[[7mxb]], [[7mxj]], [[7mxk]] - Chk PknG kinase domain + AMPPNP - Corynebacterium glutamicum
*'''hChk Nek'''
**[[4apc]] – hChk Nek1 kinase domain (mutant)
**[[4b9d]] - hChk Nek1 kinase domain (mutant) + inhibitor
**[[2w5h]] – hChk Nek2 kinase domain
**[[2jav]], [[2wqo]], [[2xk3]], [[2xk4]], [[2xk6]], [[2xk7]], [[2xk8]], [[2xkc]], [[2xkd]], [[2xke]], [[2xkf]], [[2xnm]], [[2xnn]], [[2xno]], [[2xnp]], [[4a4x]], [[4afe]], [[5m51]], [[5m53]], [[5m55]], [[5m57]], [[6sgd]], [[6sgh]], [[6sgi]], [[6sgk]], [[6sk9]] – hChk Nek2 + inhibitor
**[[2w5a]], [[2w5b]] – hChk Nek2 + nucleotide
**[[6tm5]] - hChk Nek2 in anaphase-promoting complex – Cryo EM
**[[2wqm]], [[6s76]] – hChk Nek7
**[[2wqn]] – hChk Nek7 + ADP
**[[5de2]] – hChk Nek7 + hChk Nek9
**[[6s73]], [[2wqo]] – hChk Nek7 + inhibitor
**[[6npy]] – hChk Nek7 + Nlrp3
**[[6s75]] – hChk Nek7 + inhibitor
*'''Chk Rio'''
**[[6fdo]], [[6fdn]], [[6fdm]] – hChk Rio2
**[[4otp]] – hChk Rio1 Rio domain + ADP
**[[6hk6]], [[7vbt]] – hChk Rio2 + inhibitor
**[[6eml]], [[6fai]], [[6g18]], [[6g51]], [[6rbd]],[[6rbe]], [[6y7c]] – yChk Rio2 in 40S particle – Cryo EM
**[[1ztf]] – AfChk Rio1 + adenine derivative – Archaeoglobus fulgidus
**[[1zth]] – AfChk Rio1 + ADP
**[[1zp9]] – AfChk Rio1 + ATP
**[[1tqp]], [[1zao]] – AfChk Rio2 + ATP
**[[1zar]] – AfChk Rio2 + ADP
**[[4gyg]] – CtChk Rio2 – Chaetonium thermophilum
**[[4gyi]] – CtChk Rio2 + ADP
*hChk Vrk (vaccinia-related kinase)
**[[2kty]], [[2kul]], [[2lav]], [[2rsv]] – hChk Vrk1 kinase domain 1-396 - NMR
**[[3op5]] – hChk Vrk1 kinase domain (mutant)
**[[5ukf]] – hChk Vrk1 kinase domain + inhibitor
**[[5uvf]], [[6cnx]], [[6bu6]], [[6cfm]], [[6dd4]], [[6bp0]], [[6bru]], [[6btw]], [[6cmm]], [[6cqh]], [[6csw]], [[6npn]], [[6vxu]], [[6vzh]] – hChk Vrk1 kinase domain (mutant) + inhibitor
**[[6ac9]] – hChk Vrk1 kinase domain (mutant) + AMPPNP
**[[7tan]] – hChk Vrk1 kinase domain + nucleosome – Cryo EM
**[[2v62]] – hChk Vrk2 kinase domain
**[[5uu1]], [[6ncg]], [[8q1z]] – hChk Vrk2 kinase domain + inhibitor
*Chk Wnk (protein kinase lysine-deficient); Domains - kinase 194-483; CCT1 454-549
**[[6cn9]], [[4q2a]], [[4pwn]] - hChk Wnk1 kinase domain (mutant)
**[[5tf9]] - hChk Wnk1 kinase domain + inhibitor + AMPPNP
**[[5wdy]], [[5we8]] - hChk Wnk1 kinase domain + inhibitor + ANP
**[[5drb]], [[6ol2]]- rChk Wnk1 kinase domain (mutant) + inhibitor
**[[6elm]] - hChk Wnk2 CCT1 domain
**[[6fbk]] - hChk Wnk2 CCT1 domain + Wnk1 peptide
**[[5o1v]], [[5o21]], [[5o23]] - hChk Wnk3 kinase domain
**[[5o2c]] - hChk Wnk3 kinase + CCT1 domains
**[[5o26]], [[5tf9]] - hChk Wnk3 kinase domain + AMPPNP
**[[5o2b]] - hChk Wnk3 kinase domain + inhibitor
**[[8edh]] - hChk Wnk3 kinase domain (mutant) + inhibitor
**[[2lru]] – rChk Wnk1 autoinhibitory domain 480-572 - NMR
**[[5w7t]] - rChk Wnk1 kinase domain
**[[7uos]] - rChk Wnk1 kinase domain (mutant)
*'''TANK-binding kinase'''
**[[4efo]] – hChk Tbk1 ubiquitin-like domain
**[[6rsr]], [[6rsu]] – hChk Tbk1 + inhibitor
**[[4im0]], [[4im2]], [[4im3]], [[4iw0]], [[4iwo]], [[4iwp]], [[4ipq]], [[6rst]] – hChk Tbk1 (mutant) + inhibitor
**[[6cq5]], [[6cq4]], [[6cq0]], [[6boe]], [[6bod]], [[6bny]], [[5w5v]] – hChk Tbk1 + ulcer drug
**[[4eut]], [[4euu]] – hChk Tbk1 kinase+ubiquitin-like domains (mutant) + inhibitor
**[[6nt9]] – hChk Tbk1 (mutant) + STING
**[[5eoa]], [[5eof]] – hChk Tbk1 residues 677-729 + optineurin
**[[4jl9]], [[4jlc]] – mChk Tbk1 + inhibitor
**[[6o8c]], [[6o8b]] – mChk Tbk1 (mutant) + STING
*'''Haspin'''
**[[2vuw]], [[2wb8]] – hChk Haspin kinase domain
**[[3dle]] – hChk Haspin kinase domain + AMP
**[[3e7v]], [[3f2n]], [[3fmd]], [[3iq7]], [[4qtc]], [[5htb]], [[5htc]], [[6z56]], [[6z57]], [[6z58]], [[6z59]], [[6z5a]], [[6z5b]], [[6z5c]]. [[6z5d]], [[6z5e]] , [[7avq]], [[7ops]] – hChk Haspin kinase domain + inhibitor
**[[7sqm]] – hChk Haspin kinase domain + antimalarial
**[[6g38]], [[6g34]], [[6g35]], [[6g36]], [[6g37]] – hChk Haspin kinase domain + tubercidin derivative
**[[6g39]], [[6g3a]] – hChk Haspin kinase domain (mutant) + tubercidin derivative
**[[4ouc]] – hChk Haspin kinase domain + histone H3 peptide
*'''MAP/microtubule affinity-regulating kinase (MARK)'''
**[[2hak]] – hChk MARK1 catalytic+UBA domains
**[[3ose]] - hChk MARK1 KA1 domain
**[[6c9d]] – hChk MARK1 catalytic+UBA+KA1 domains (mutant)
**[[5eak]], [[5kz7]], [[5kz8]] – hChk MARK2 catalytic+UBA domains + inhibitor
**[[3iec]] – hChk MARK2 catalytic+UBA domains + cytotoxicity-associated immunodominant antigen peptide
**[[2qnj]] – hChk MARK3 catalytic+UBA domains
**[[3fe3]] – hChk MARK3 catalytic+UBA domains (mutant)
**[[7p1l]] – hChk MARK3 catalytic+UBA domains + inhibitor
**[[5es1]] – hChk MARK4 catalytic+UBA domains + inhibitor
**[[1zmu]] – rChk MARK2 catalytic+UBA domains
**[[2wzj]], [[2r0i]], [[1zmv]], [[1y8g]], [[1zmw]] – rChk MARK2 catalytic+UBA domains (mutant)
**[[1ul7]], [[1v5s]] - mChk MARK3 catalytic domain - NMR
*'''Mitotic checkpoint Chk (Bub)'''; Domains: TPR 1-220; kinase 726-1085
**[[2lah]] – hChk Bub1 TPR domain – NMR
**[[2wvi]] – hChk Bub1β TPR domain
**[[3si5]] – hChk Bub1 TPR domain + CASC5 peptide
**[[4r8q]], [[4qpm]], [[5dmz]] – hChk Bub1 kinase domain + ADP
**[[6f7b]] – hChk Bub1 kinase domain + inhibitor
**[[4a1g]] – hChk Bub1 TPR domain + CASC5 KI motif
**[[4ggd]] - hChk Bub1 + cell division cycle protein
**[[6tlj]], [[5khu]] - hChk Bub1 in anaphase-promoting complex – Cryo EM
**[[6jkk]] – DmChk Bub1 kinase domain
**[[6jkm]] – DmChk Bub1 kinase domain + ADP
**[[5jja]] – hChk Bub1 residues 661-734 + PP2A
**[[3esl]] – yChk Bub1 N terminal
**[[4bl0]] - yChk Bub1 + cell cycle arrest protein Bub3
*'''Microtubule-associated Chk'''
**[[2m9x]] – hChk 1 residues 187-287 – NMR
**[[3ps4]] - hChk 1 residues 965-1057
**[[2kqf]], [[2kyl]] – hChk 2 PDZ domain + glycoprotein C terminal – NMR
**[[3khf]] - hChk 3 PDZ domain
**[[2w7r]] – hChk 4 PDZ domain
*'''mTOR''' or '''Mechanistic target of rapamycin'''
*''mTOR FRB domain residues 2015-2114''
**[[1nsg]], [[1fap]] – hFRAP FRB domain + FKBP
**[[2rse]] – hFRAP FRB domain + FKBP – NMR
**[[1aue]] – hFRAP FRB domain
**[[2gaq]], [[2npu]] – hFRAP FRB domain - NMR
**[[8ppz]] – hFRAP FRB domain + FKBP + pyridine derivative
**[[3fap]], [[2fap]], [[4fap]] – hFRAP FRB domain + FKBP + rapamycin analog
**[[4drh]], [[4dri]], [[4drj]], [[5gpg]] – hFRAP FRB domain + FKBP + rapamycin
**[[6m4u]], [[6m4w]] – hChk Mtor FRB domain (mutant) + FKBP1A + rapamycin
**[[5wbh]] – hFRAP FRB domain + S6K1 peptide
*''mTOR FAT+PIKK domain residues 1376-2549''
**[[4jsn]] – hFRAP + TORC subunit LST8
**[[4jsp]] – hFRAP + TORC subunit LST8 + ATP
**[[4jsv]] – hFRAP + TORC subunit LST8 + ADP
**[[4jsx]] – hFRAP + TORC subunit LST8 + torin2
**[[4jt5]] – hFRAP + TORC subunit LST8 + pp242
**[[4jt6]] – hFRAP + TORC subunit LST8 + PI-103
**[[5wby]], [[5wbu]] – hFRAP + TORC subunit LST8 + proline-rich Akt1 substrate
*''mTOR complex''
**[[5flc]] – hmTOR + RAPTOR + LST8 + FKBP – Cryo EM
**[[5h64]] – hmTOR + RAPTOR + LST8 – Cryo EM
**[[6sb2]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC – Cryo EM
**[[6sb0]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC + proline-rich Akt1 substrate – Cryo EM
**[[5zcs]] – hmTOR + LST8 + AVO3 + TORC2 – Cryo EM
**[[7tzo]] – hTORC2 in mTORC2 complex– Cryo EM
**[[6zwm]], [[6zwo]], [[7owg]], [[7pe7]], [[7pe8]], [[7pe9]], [[7pea]], [[7peb]], [[7pec]], [[7uxc]] , [[8era]]– mTOR in mTor complex – Cryo EM
*'''Gcn2'''
**[[1zyc]] – yChk Gcn2
**[[1zxe]], [[1zy4]], [[1zy5]] – yChk Gcn2 (mutant)
**[[2yz0]] – yChk Gcn2 RWD/GI domain – NMR
**[[4otm]] – yChk Gcn2 C terminal domain
**[[1zyd]] – yChk Gcn2 + ATP
**[[4otn]] – mChk Gcn2 C terminal domain
*'''LRRK1''' or leucine-rich repeat Chk1
**[[8e04]], [[8e05]], [[8e06]], [[8fac]] – hLRRK1 – Cryo EM
*'''LRRK2''' or leucine-rich repeat Chk2 or dardarin
**[[6xr4]] – hLRRK2 – Cryo EM
**[[7lht]], [[7lhw]], [[7li4]] – hLRRK2 + ATP + GDP – Cryo EM
**[[7li3]] – hLRRK2 (mutant) + ATP + GDP – Cryo EM
**[[6oje]], [[7thy]] – hLRRK2 GTPase domain 1329-1520
**[[6ojf]] – hLRRK2 GTPase domain (mutant)
**[[6dlo]], [[6dlp]] – hLRRK2 WD40 domain
**[[7thz]] – hLRRK2 1330-1527 + GDP
**[[6vno]], [[6vp6]], [[6vp7]] – hLRRK2 C terminal 1330-2527 – Cryo EM
**[[6vp8]] – hLRRK2 C terminal 1330-2527 + COR domain 1670-1950 + WD40 domain 2140-2489 – Cryo EM
**[[6s6q]] – AtLRRK2 ectodomain + protein casparian strip peptide
*'''Pim'''
*Pim1 catalytic domain residues 14-313
**[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain
**[[1yxs]] – hPim1 catalytic domain (mutant)
**[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP
**[[1yxu]] – hPim1 catalytic domain + AMP
**[[1yxv]], [[5ipj]] – hPim1 catalytic domain + quinoline derivative
**[[1yxx]] – hPim1 catalytic domain + indole derivative
**[[2bzh]], [[2bzi]], [[2bzj]] – hPim1 catalytic domain (mutant) + organometallic ligand
**[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3c4e]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umw]], [[3umx]], [[4enx]], [[4eny]], [[4k1b]], [[4k18]], [[4k0y]], [[4iaa]], [[4i41]], [[4ll5]], [[4lm5]], [[4lmu]], [[4mta]], [[4med]], [[4mbl]], [[4mbi]], [[4n6y]], [[4n6z]], [[4n70]], [[4xh6]], [[5iis]], [[5kgd]], [[5kge]], [[5kgg]], [[5kgi]], [[5kgk]], [[5kzi]], [[5vua]], [[5vub]], [[5vuc]], [[6mt0]], [[6vrv]], [[7oov]], [[7oow]], [[7oox]], [[7xsv]] – hPim1 catalytic domain + inhibitor
**[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor
*Pim1 kinase domain residues 92-404
**[[4jx3]] – hPim1 kinase domain
**[[3uix]], [[5c1q]] – hPim1 kinase domain residues 120-404 + quinoline derivative
**[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate
**[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand
**[[1xws]], [[4alu]], [[4alv]], [[4alw]], [[4as0]], [[4bzn]], [[4bzo]], [[4dtk]], [[4jx7]], [[4rbl]], [[4rc2]], [[4rc3]], [[4rc4]], [[4ty1]], [[4wrs]], [[4wsy]], [[4wt6]], [[4xhk]], [[5dgz]], [[5dhj]], [[5dia]], [[5dwr]], [[5eol]], [[5kcx]], [[5o11]], [[5o12]], [[5o13]], [[5tel]], [[5tex]], [[5toe]], [[5v80]], [[5v82]]. [[6bsk]], [[6kzi]], [[6l11]], [[6l12]], [[6l13]], [[6l14]], [[6l15]], [[6l16]], [[6l17]], [[6no8]], [[6no9]], [[6vru]], [[6ykd]], [[7zun]] – hPim1 kinase domain + inhibitor
**[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor
*Pim1 full length
**[[4rpv]], [[5tur]] - hPim1 + inhibitor
*Pim1 complex with consensus peptide (pimtide)
**[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6qxk]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]] – hPim1 kinase domain + inhibitor + consensus peptide
**[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide
**[[2c3i]], [[5ndt]], [[5n5m]], [[5n5l]], [[5n52]], [[5n51]], [[5n50]], [[5n4z]], [[5n4y]], [[5n4x]], [[5n4v]], [[5n4u]], [[5n4r]], [[5n4o]], [[5n4n]], [[5mzl]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide
**[[4gw8]], [[7qb2]], [[7qfm]], [[7z6u]], [[8afr]] – hPim1 catalytic domain (mutant) + inhibitor + pimtide
**[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide
**[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide
*Pim1 containing phosphorylated Ser 261
**[[1yhs]] – hPim1 kinase domain + PSer + staurosporine
**[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor
**[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor
**[[1yi4]] – hPim1 kinase domain + PSer + adenosine
*Pim2
**[[4x7q]] – hPim2 catalytic domain + inhibitor
**[[2iwi]] – hPim2 catalytic domain + Ru ligand
*'''Rip or receptor-interacting Chk; Domains – catalytic 1-294; Amyloid fibril 418-518; Death 561-671'''
**[[6ac5]] – hRip1 death domain
**[[6r5f]], [[6nw2]], [[6c4d]], [[6c3e]], [[5tx5]], [[7fcz]], [[7fd0]], [[7ydx]] – hRip1 catalytic domain + inhibitor
**[[6rln]], [[6ocq]], [[6nyh]], [[6hho]] – hRip1 catalytic domain (mutant) + inhibitor
**[[6ggs]] – hRip2 – Cryo EM
**[[5yrn]] – hRip2 CARD domain 434-540 – Cryo EM
**[[6szj]], [[6sze]], [[6s1f]], [[6rna]], [[6rn8]], [[6hmx]], [[6fu5]], [[6es0]], [[5w5o]], [[5w5j]] – hRip2 catalytic domain + inhibitor
**[[6ul8]] – hRip2 catalytic domain (mutant) + inhibitor
**[[8aza]] – hRip2 catalytic domain + XiaP Bir2 domain – Cryo EM
**[[7mx3]] – hRip3 catalytic domain (mutant) + inhibitor
**[[7mon]] – hRip3 catalytic domain (mutant) + MLKL
**[[7dac]] – hRip3 amyloid fibril - NMR
**[[7da4]] – hRip3 amyloid fibril – Cryo EM
**[[6oko]] – mRip3 catalytic domain + inhibitor
**[[6jpd]] – mRip3 residues 409-486 - NMR
**[[5wnm]], [[5wnj]] – mRip4 catalytic domain (mutant) + drug
**[[5wnl]] – mRip4 catalytic domain (mutant) + staurosporine
**[[5wnk]] – mRip4 catalytic domain (mutant) + inhibitor
**[[5wni]] – mRip4 catalytic domain (mutant) + ATP
**[[6gwm]] – rRip2 caspase recruitment domain 433-539
*'''Ulk'''
**[[6qas]] – hChk Ulk1 + inhibitor
**[[5ci7]], [[6mnh]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[8soi]], [[8sqz]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein
**[[8srm]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein – Cryo EM
**[[8srq]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein + PI3K – Cryo EM
**[[6qav]], [[6qau]], [[6qat]], [[6yid]] – hChk Ulk2 + inhibitor
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[6fdz]], [[6fdy]] – hChk Ulk3 + leukemia drug
**[[6tsz]] – hChk Ulk4 pseudfokinase domain + ATPgS
**[[6u5l]] – hChk Ulk4 (mutant) + inhibitor
*'''Hipa''' and '''Hipb'''
**[[3tpd]], [[3tpe]] – EcChk Hipa – ''Escherichia coli''
**[[3tpb]], [[3dnt]], [[3dnu]] – EcChk Hipa (mutant)
**[[4pu7]], [[4pu8]] – SoChk Hipb - ''Shewanella oneidensis''
**[[3tpt]] – EcChk Hipa (mutant) + ADP
**[[3fbr]] – EcChk Hipa (mutant) + AMPPNP + peptide
**[[3tpv]] – EcChk Hipa + ADP
**[[2wiu]] – EcChk Hipa + Hipb
**[[4yg7]], [[5k98]], [[3hzi]], [[3dnv]] – EcChk Hipa + Hipb + DNA
**[[4yg1]], [[4z58]], [[4z59]], [[4z5c]], [[4z5d]] – EcChk Hipb + DNA
**[[4z5h]] – EcChk Hipb (mutant) + DNA
**[[4pu3]], [[4pu4]] – SoChk Hipa + Hipb + DNA - ''Shewanella oneidensis''
**[[4pu5]] – SoChk Hipa + AMPPNP
*'''Chk Smg'''
**[[6l53]] – hChk Smg1 – Cryo EM
**[[7pw6]] – hChk Smg1 + inhibitor – Cryo EM
**[[7pw7]] – hChk Smg1 + Smg9 + inhibitor – Cryo EM
**[[7pw9]] – hChk Smg1 + Smg9 + AMPPNP + ATP – Cryo EM
**[[6l54]], [[6syt]] – hChk Smg1 + Smg8 + Smg9 – Cryo EM
**[[7pw4]], [[7pw5]] – hChk Smg1 + Smg8 + Smg9 + inhibitor – Cryo EM
**[[7pw8]] – hChk Smg1 + Smg8 + Smg9 + AMPPNP – Cryo EM
**[[6z3r]] – hChk Smg1 + Smg8 + Smg9 + regulator of nonsense transcripts – Cryo EM
**[[2hwy]] – hChk Smg5 PIN domain
**[[2hww]], [[2hwx]] – hChk Smg6 PIN domain (mutant)
**[[4um2]] – hChk Smg6 TPR domain
**[[1ya0]] – hChk Smg7 N terminal
*'''Chk Vprbp or DCAF1'''
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain 1039-1401 (mutant)
**[[7sse]], [[7ufv]], [[8f8e]], [[8og5]], [[8og6]], [[8og7]], [[8og8]], [[8og9]], [[8oga]], [[8ogb]], [[8ogc]], [[8oo5]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) + inhibitor
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[5aja]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
*'''Other Chk'''
**[[1wak]] – hChk Sprk1
**[[3dak]] – hChk Osr1 kinase domain
**[[7okw]] – hChk Osr1 C-terminal
**[[4aw2]] – hChk Mrckα kinase domain
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain (mutant)
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[1uf0]] – hChk Dcamkl1 DCX domain – NMR
**[[1u5q]] – rChk Tao2 kinase domain
**[[2cos]] – mChk Lats2 – NMR
**[[1xte]], [[1xtn]], [[6edx]] – mChk Sgk3 PX domain
**[[4yom]] – mChk Brsk2
**[[4ynz]] – mChk Brsk1 N terminal domain
**[[5iri]] – mChk Brsk1 residues 592-719
**[[5oat]], [[7mp8]] – rfbChk Pink1– red flour beetle
**[[7t3x]] – Chk Pink1 (mutant) – louse
**[[4f0g]] – smChk Roco4 kinase domain – slime mold
**[[5tos]] – AtChk Bik1
**[[1q8z]], [[1zyc]] – yChk
**[[1how]], [[1zxe]], [[1zy4]] – yChk (mutant)
**[[1ow5]], [[1x9x]] – yChk Ste11 SAM domain – NMR
**[[2kio]], [[2kit]], [[1w1n]] – yChk Tor1 FATC domain – NMR
**[[3gre]] – yChk Vps15 WD repeat domain
**[[3osm]], [[3ost]] - yChk Kcc4 kinase domain
**[[5yyx]] – yChk Mek1 FHA domain
**[[6jxc]], [[6jxa]] – yChk Tel1 – Cryo EM
**[[6u69]] – CaChk Yck2 – ''Candida albicans''
**[[6sl1]], [[6sl0]], [[6skz]], [[6sky]] – Chk Tel1 – ''Chaetonium thermophilum'' – Cryo EM
**[[6ra0]] – CeChk Dkf1 – ''Chaenorhabditis elegans''
**[[7z6e]] – CeChk Mrck1 regulatory domain
**[[6tlb]] – Chk – ''Plasmodium falciparum''
*Other Chk complexes
**[[1wbp]], [[7dd1]] – hChk Sprk1 + peptide
**[[3beg]] – hChk Srpk1 + splicing factor SF2
**[[3hdm]], [[3hdn]], [[7pue]] – hChk Sgk1 (mutant) + inhibitor
**[[2r5t]] – hChk Sgk3 + AMPPNP
**[[4yff]], [[4yfi]], [[6b5j]], [[7mgj]], [[7mgk]] – hChk Tnni3k + inhibitor
**[[2v3s]] – hChk Osr1 + hChk Wnk4 peptide
**[[2vwi]] – hChk Osr1 kinase domain + ANP
**[[7que]], [[7quf]] – hChk Drak1 kinase domain + inhibitor
**[[4crs]] – hChk N2 kinase domain + ATPγS
**[[3tku]], [[4ual]], [[3qfv]], [[5ote]], [[5otf]] – hChk Mrckβ + inhibitor
**[[4uak]] – hChk Mrckβ + ADP
**[[5aja]], [[4z8l]], [[4cc9]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
**[[5jk7]] – hChk Vprbp WD repeat domain + VPX + DDB1 + UDG
**[[3wa0]], [[4p7i]] – hChk Vprbp residues 1417-1506 + merlin
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[5ci7]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[5b5w]], [[5b6b]], [[5brk]] – hChk Lats1 residues 622-704 + MOB1
**[[5yz0]] – hChk Atr + Atr-interacting protein – Cryo EM
**[[6bdn]] – hChk Tao3 kinase domain + ADP
**[[5yh3]] – hChk Fam20C 141-578 + pseudokinase Fam20A
**[[2gcd]] – rChk Tao2 kinase domain + staurosporine
**[[1u5r]] – rChk Tao2 kinase domain + ATP
**[[5yj9]], [[7mp9]] – rfbChk Pink1 kinase domain + AMPPNP
**[[6bn1]] – DmChk Hippo SARAH domain + Shar-Pei
**[[3hgk]] – Chk Pto + effector protein AVRPTOB – Currant tomato
**[[3p86]], [[3ppz]] - AtChk Ctr1 + staurosporine
**[[4f0f]] – smChk Roco4 kinase domain + APPCP
**[[4f1m]], [[4f1o]] – smChk Roco4 kinase domain (mutant) + APPCP
**[[4f1t]], [[4yzm]], [[4yzn]] – smChk Roco4 kinase domain + inhibitor
**[[5fvm]] - Tor2 + LST8 - ''Kluyveromyces marxianus''
**[[5kc2]] - yVps15 + Vps34 - Cryo EM
**[[5dfz]] - yVps15 + Vps34 + Vps30 + VPSAP28 + VPSAP30 - Cryo EM
**[[1q8y]], [[1q97]], [[1q99]], [[1zyd]] – yChk + nucleotide
**[[1zy5]] – yChk (mutant) + nucleotide
**[[2jd5]] – yChk + NPL-3P
**[[4lqs]], [[4lqq]], [[4lqp]] – yChk Cbk1 residues 251-756 + Cbk1 activator Mob2
**[[6emk]] – yChk Tor2 + LST8 + TSC11 + AVO1 + AVO2 – Cryo EM
**[[6s8f]] – yChk Tel1 + AMPPNP – Cryo EM
**[[5yyz]] – yChk Mek1 FHA domain + Hop1
**[[5x6o]], [[6z3a]], [[7wzr]], [[7wzw]]– yChk Mec1 + LCD1 – Cryo EM
**[[6z2w]], [[6z2x]] – yChk Mec1 (mutant) + LCD1 – Cryo EM
**[[7kue]] – yChk Kin28 in TFIIK complex – Cryo EM
**[[6u6a]] – CaChk Yck2 + inhibitor
**[[5fvm]] – Chk Tor2 + LST8 – ''Kluyveromyces maximanus''
*Serine/threonine protein kinase Rad53 see [[Rad53]]
*Serine/threonine protein kinase Gsk3B see [[Glycogen synthase kinase 3]]
}}
[[Category:Topic Page]]

Serine/threonine protein kinase 3D structures

2026-08-19T07:23:29Z

Michal Harel:

==3D structures of serine/threonine protein kinase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Chk1'''; domains - kinase 1-289; KA1 393-492
**[[1ia8]] – hChk1 kinase domain – human
**[[5w12]] – hChk1 KA1 domain
**[[1zlt]] – hChk1 kinase domain + hymenaldisine
**[[1nvq]], [[1nvr]] – hChk1 kinase domain + peptide + saurosporine
**[[1nvs]], [[1zys]], [[7ako]] - hChk1 kinase domain + peptide + inhibitor
**[[7akm]] - hChk1 kinase domain + ATP
**[[2ayp]], [[2br1]], [[2brb]], [[2brg]], [[2brh]], [[2brm]], [[2brn]], [[2bro]], [[2c3j]], [[2c3k]], [[2c3l]], [[2cgu]], [[2cgv]], [[2cgw]], [[2cgx]], [[2e9n]], [[2e9o]], [[2e9p]], [[2e9u]], [[2e9v]], [[2gdo]], [[2ghg]], [[2hog]], [[2hxl]], [[2hxq]], [[2hy0]], [[2qhm]], [[2qhn]], [[2r0u]], [[3f9n]], [[2wmq]], [[2wmr]], [[2wms]], [[2wmt]], [[2wmu]], [[2wmv]], [[2wmw]], [[2wmx]], [[2xey]], [[2xf0]], [[2xez]], [[2x8d]], [[2x8e]], [[2x8i]], [[2ydi]], [[2ydj]], [[2ydk]], [[2yer]], [[2yex]], [[2ym3]], [[2ym4]], [[2ym5]], [[2ym6]], [[2ym7]], [[2ym8]], [[2ywp]], [[3jvr]], [[3jvs]], [[3nlb]], [[3ot3]], [[3ot8]], [[3pa3]], [[3pa4]], [[3pa5]], [[3tkh]], [[3tki]], [[3u9n]], [[4fsm]], [[4fsn]], [[4fsq]], [[4fsr]], [[4fst]], [[4fsu]], [[4fsw]], [[4fsy]], [[4fsz]], [[4ft0]], [[4ft3]], [[4ft5]], [[4ft7]], [[4ft9]], [[4fta]], [[4ftc]], [[4fti]], [[4ftj]], [[4ftk]], [[4ftl]], [[4ftm]], [[4ftn]], [[4fto]], [[4ftq]], [[4ftr]], [[4ftt]], [[4ftu]], [[4gh2]], [[4hyh]], [[4hyi]], [[4jik]], [[4qye]], [[4qyf]], [[4qyg]], [[4qyh]], [[4rvk]], [[4rvl]], [[4rvm]], [[5dls]], [[5f4n]], [[5fcf]], [[5fck]], [[6fc8]], [[6fcf]], [[6fck]], [[7bko]], [[8e80]], [[8e81]] - hChk1 kinase domain + inhibitor 
**[[5oot]], [[5op2]], [[5op4]], [[5op5]], [[5op7]], [[5opb]], [[5opr]], [[5ops]], [[5opu]], [[5opv]], [[5oq5]], [[5oq6]], [[5oq7]], [[5oq8]], [[7bjd]], [[7bjh]], [[7bjj]], [[7bjm]], [[7bjo]], [[7bjr]], [[7bjx]], [[7bk1]], [[7bk2]], [[7bk3]], [[7mck]], [[7suf]], [[7sug]], [[7suh]], [[7sui]], [[7suj]], [[8siv]], [[8siw]], [[8six]] - hChk1 kinase domain (mutant) + inhibitor
**[[5oop]] - hChk1 kinase domain (mutant) + AMPPNP
**[[5oor]] - hChk1 kinase domain (mutant) + staurosporine
**[[7bkn]] - hChk1 kinase domain + adenine
**[[7bje]] - hChk1 kinase domain (mutant) + adenine
**[[2jqi]] – yChk1 – yeast
*'''Chk2 (Checkpoint kinase)'''
**[[1gxc]] – hChk2 phosphothreonine-binding domain + phosphopeptide
**[[2cn5]] – hChk2 kinase domain + ADP
**[[2cn8]] – hChk2 kinase domain + inhibitor
**[[2cn8]], [[2uv2]], [[2w0j]], [[2w7x]], [[2wtc]], [[2wtd]], [[2wti]], [[2wtj]], [[2xbj]], [[2xk9]], [[2xm8]], [[2xm9]], [[2ycf]], [[2ycq]], [[2ycr]], [[2ycs]], [[2yiq]], [[2yir]], [[2yit]], [[4a9r]], [[4a9s]], [[4a9t]], [[4bda]], [[4bdb]], [[4bdc]], [[4bdd]], [[4bde]], [[4bdf]], [[4bdg]], [[4bdh]], [[4bdi]], [[4bdj]], [[4bdk]] - hChk2 kinase domain + inhibitor
**[[3i6u]], [[3i6w]] – hChk2 residues 84-502 (mutant)
*'''Chk3 (Mst2)'''; domains - kinase 13-313; SARAH 436-484
**[[3wws]], [[4hkd]], [[4l0n]], [[4oh9]] – hChk3 SARAH domain 
**[[4lg4]] – hChk3 kinase domain
**[[4lgd]] – hChk3 kinase domain + RASSF5 SARAH domain
**[[6ao5]] – hChk3 kinase+SARAH domains (mutant) + SAV1 SARAH domain
**[[5dh3]], [[8a66]] – hChk3 kinase domain + inhibitor
*'''Chk4 (Mst1)''' ; Domains – kinase 1-311; SARAH 432-480
**[[3com]] – hChk4 kinase domain
**[[6yat]], [[8a5j]]– hChk4 kinase domain + inhibitor
**[[4nr2]] – hChk4 SARAH domain
**[[2jo8]] – hChk4 SARAH domain - NMR
**[[4oh8]] – hChk4 SARAH domain + Ras association domain-containing protein
*'''Chk5 (Aurora kinase b)'''
**[[4af3]] – hChk5 + inhibitor
*'''Chk6 or Chk15 or Aurora kinase A'''
**[[1mq4]], [[1muo]], [[4j8n]], [[4o0s]], [[6cpe]] – hChk6 kinase domain 
**[[1muo]], [[1mq4]], [[4j8n]], [[6cpe]], [[4o0s]] – hChk6 kinase domain
**[[4bn1]], [[4o0w]], [[4o0u]] – hChk6 kinase domain (mutant)
**[[5dnr]], [[5drd]], [[5dt3]] – hChk6 kinase domain + ATP
**[[5drd]] – hChk6 kinase domain + ATP
**[[1ol6]] – hChk6 kinase domain (mutant) + ATP
**[[2wqe]] – hChk6 kinase domain (mutant) + ADP
**[[5odt]] – hChk6 kinase domain (mutant) + ADP + TACC3
**[[2c6d]] – hChk6 kinase domain (mutant) + ADPNP
**[[2dwb]] – hChk6 kinase domain + AMPPNP
**[[6cpf]] – hChk6 kinase domain + AMPPCP
**[[5g15]] – hChk6 kinase domain + AMPPNP + monobody
**[[6cpg]], [[8ssp]] – hChk6 kinase domain + inhibitor + monobody
**[[2j4z]], [[2j50]], [[2np8]], [[3efw]], [[2x81]], [[2x6d]], [[2x6e]], [[3myg]], [[3vap]], [[4b0g]], [[4j8m]], [[5dpv]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5one]], [[5obr]], [[4byi]], [[4byj]], [[4jai]], [[4jaj]], [[3w10]], [[3w16]], [[3w18]], [[3w2c]], [[4uzh]], [[4uzd]], [[4uyn]], [[4zs0]], [[4ztq]], [[4ztr]], [[4zts]], [[5aad]], [[5aae]], [[5aag]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5obr]], [[5one]], [[6gra]], [[6c2t]], [[6c2r]], [[5zan]], [[6z4y]], [[7ayh]], [[7ayi]], [[7fic]], [[7o2v]], [[8jmx]] – hChk6 kinase domain + inhibitor
**[[2bmc]], [[2c6e]], [[3coh]], [[3h0y]], [[3h0z]], [[3h10]], [[3fdn]], [[2wtw]], [[3lau]], [[3nrm]], [[2xne]], [[2xng]], [[2xru]], [[3k5u]], [[3m11]], [[3p9j]], [[3r21]], [[3r22]], [[3qbn]], [[3unz]], [[3uo4]], [[3uo5]], [[3uo6]], [[3uod]], [[3uoh]], [[3uoj]], [[3uok]], [[3uol]], [[3up2]], [[3up7]], [[4dhf]], [[4dea]], [[4deb]], [[4ded]], [[4dee]], [[5aad]], [[5aae]], [[5aaf]], [[5aag]], [[4jbo]], [[4jbp]], [[4jbq]], [[4prj]], [[5dpv]], [[6hjk]], [[6hjj]] – hChk6 kinase domain (mutant) + inhibitor
**[[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[5dos]], [[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5dn3]], [[5dos]], [[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[6c83]] – hChk6 kinase domain + AMPPCP + nanobody
**[[8sso]] – hChk6 kinase domain + drug + monobody
**[[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5g1x]], [[7ztl]] – hChk6 kinase domain (mutant) + N-Myc
**[[8guw]] – hChk6 kinase domain/activator peptide
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + Targeting protein for XKLP2
**[[3daj]], [[3d14]], [[3dj5]], [[3dj6]], [[3dj7]], [[3d15]], [[3d2i]], [[3d2k]] – Chk6 kinase domain (mutant) + inhibitor - mouse
*Chk6 with phosphorylated Thr 287, Thr288
**[[1ol5]], [[1ol7]] – hChk6 kinase domain + PThr + ADP
**[[5dnr]], [[5dt3]] – hChk6 kinase domain + PThr + ATP
**[[2w1c]], [[2w1d]], [[2w1e]], [[2w1f]], [[2w1g]], [[5dn3]] – hChk6 kinase domain + PThr + inhibitor
**[[2wtv]], [[5orl]], [[5orn]], [[5oro]], [[5orp]], [[5orr]], [[5ors]], [[5ort]], [[5orv]], [[5orw]], [[5orx]], [[5ory]], [[5orz]], [[5os0]], [[5os1]], [[5os2]], [[5os3]], [[5os4]], [[5os5]], [[5os6]], [[5osd]], [[5ose]], [[5osf]] – hChk6 kinase domain (mutant) + PThr + inhibitor
**[[3e5a]], [[3ha6]] – hChk6 kinase domain + PThr + inhibitor + targeting protein for XKLP2
**[[5g1x]] – hChk6 kinase domain (mutant) + PThr + N-Myc
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + PThr + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + PThr + TPX2
**[[6r4d]], [[6r4c]], [[6r4b]], [[6r4a]] – hChk6 kinase domain + PThr + inhibitor + ADP
**[[6i2u]] – hChk6 kinase domain (mutant) + PThr + inhibitor + ADP
**[[6r49]] – hChk6 kinase domain (mutant) + PThr + CoA
*'''Chk10 (lymphocyte-oriented kinase)''' or LOK or STK10
**[[7qgp]] – hChk10
**[[2j7t]], [[4aot]], [[4equ]], [[4usd]], [[4use]], [[5ajq]], [[5owq]], [[5owr]], [[6eim]], [[6gtt]], [[6i2y]], [[6hxf]] – hChk10 kinase domain + inhibitor
**[[4bc6]], [[6i2y]] – hChk10 + drug
*'''Chk11'''
**[[2wtk]] – hChk11 (mutant) + calcium-binding protein
*'''Chk12-A (Aurora kinase b-a or Aurora B kinase)'''
**[[2vgo]], [[2vgp]], [[2vrx]], [[3ztx]], [[4c2v]], [[5eyk]] – fChk12-A + inner centromere protein A peptide + inhibitor - frog
**[[4c2w]] – fChk12-A + inner centromere protein A peptide + AMPPNP
**[[4b8l]], [[4b8m]], [[5k3y]] – fChk12-A (mutant) + inner centromere protein A peptide + inhibitor
*'''Chk13 (Polo-like kinase Plk)'''
*Plk1 Polo-box domain (Pbd) 371-594''
**[[1q4o]], [[2ogq]], [[3hih]], [[3p2w]], [[4h5x]], [[6n46]] – hPlk1 Pbd
*Plk1 Pbd complex with polypeptide
**[[1umw]], [[2ojx]], [[3bzi]], [[3c5l]], [[3rq7]], [[4dfw]], [[4whl]], [[4whk]], [[4whh]], [[4rcp]], [[4o6w]], [[4o56]], [[5dms]], [[5dmv]], [[5dnj]] , [[7mso]], [[7mx1]] – hPlk1 + peptide
**[[3hik]], [[3fvh]], [[3p2z]], [[3p34]], [[3p35]], [[3p36]], [[3p37]], [[3q1i]], [[4e67]], [[4e9c]], [[4e9d]], [[4hab]], [[4hy2]], [[4o9w]], [[4x9r]], [[4x9v]], [[4x9w]], [[5j19]], [[6gy2]] – hPlk1 + phosphopeptide
**[[1q4k]] – hPlk1 (mutant) + phosphopeptide
**[[2v5q]] – hPlk1 + design ankyrin repeat protein
**[[4lkl]] – hChk Plk1 + PL-55
**[[4lkm]] – hChk Plk1 + PL-74
**[[6ax4]] – hChk Plk1 + histidine cyclized macrocycle
**[[5x3s]] – mPlk1 + phosphopeptide
**[[8joq]], [[8joy]] – hPlk1 Pbd + hpv peptide
*Plk1 Pbd complex with small molecule inhibitor
**[[4h71]], [[4hco]], [[5ta6]], [[5ta8]], [[8bjt]], [[8crc]] – hPlk1 + inhibitor
**[[2rku]] – hPlk1 (mutant) + inhibitor
**[[3db6]], [[3db8]], [[3dbc]], [[3dbd]], [[3dbe]], [[3dbf]] – zfPlk1 (mutant) + inhibitor – zebra fish
*Plk1 catalytic domain 36-345
**[[2owb]] – hPlk1 catalytic domain (mutant)
**[[2ou7]] – hPlk1 catalytic domain (mutant) + AM
**[[3kb7]], [[2yac]], [[3thb]], [[4a4l]], [[4a4o]] – hPlk1 catalytic domain + inhibitor
**[[3fc2]] – hPlk1 catalytic domain (mutant) + inhibitor
**[[4j52]], [[4j53]] – hChk Plk1 (mutant) + inhibitor
**[[3d5x]] – zfPlk1 catalytic domain (mutant) + wortmannin
**[[3d5w]] – zfPlk1 catalytic domain + ADP
*'''Plk2'''
**[[4i5m]], [[4i5p]], [[4i6b]], [[4i6f]], [[4i6h]] – hChk Plk2 kinase domain (mutant) + inhibitor
**[[4xb0]], [[4rs6]] – hChk Plk2 Pbd
*'''Plk3'''
**[[4b6l]], [[4i6b]] – hChk Plk3 kinase domain + inhibitor
*'''Plk4'''; Domains – kinase 2-275; Pbd 580-808; Pb3 884-970
**[[3cok]] – hChk Plk4 kinase domain
**[[4n9j]] – hChk Plk4 Pbd domain
**[[4n7z]], [[4n7v]] – hChk Plk4 Pbd domain + centrosomal protein
**[[6w38]], [[6w3i]] – hChk Plk4 Pbd domain + Fam46C
**[[6w3j]] – hChk Plk4 Pbd domain + Fam46C + CEP92 peptide
**[[4jxf]], [[4yur]] – hChk Plk4 kinase domain + inhibitor
**[[5lhy]] – hChk Plk4 Pb3 domain
**[[4yyp]], [[5lhz]] – hChk Plk4 Pb3 domain + Scl-interrupting locus protein
**[[4nk7]], [[4g7n]], [[5lhx]], [[7rl3]] – DmChk Plk4 Pbd domain – ''Drosophila melanogaster''
*'''Chk16'''
**[[2buj]] – hChk16 (mutant) + staurosporin
*'''Chk17B''' or DRAK2 or STK17B
**[[3lm0]] – hChk17B
**[[6qf4]], [[7q7c]], [[7q7d]] – hChk17B + ADP
**[[7q7e]] – hChk17B + ATP
**[[3lm5]] – hChk17B + quercetin
**[[6y6f]], [[6y6h]], [[6zjf]] – hChk17B + pyrimidine derivative
**[[7akg]] – hChk17B + drug
*'''Chk19''' or STK19
**[[7xrb]] – hChk19
*'''Chk24 (Mst3)''' or STK24
**[[3a7f]], [[3a7g]], [[3a7h]], [[3a7i]], [[3a7j]], [[3ckw]] – hChk24 kinase domain
**[[4w8e]], [[4w8d]], [[4u8z]], [[4qmm]], [[4qmn]], [[4qmo]], [[4qmp]], [[4qmq]], [[4qms]], [[4qmt]], [[4qmu]], [[4qmv]], [[4qmw]], [[4qmx]], [[4qmy]], [[4qmz]], [[4qna]], [[4qo9]], [[4u8z]], [[7b30]], [[7b31]], [[7b32]], [[7b33]], [[7b34]], [[7b35]], [[8bzi]], [[8bzj]], [[8qlr]], [[8qls]], [[8qlt]] – hChk Mst3 + inhibitor
**[[8qlq]] – hChk Mst3 + macrocyclic inhibitor
**[[3ckx]] – hChk24 kinase domain + staurosporin
**[[3zhp]] – hChk24 kinase domain + calcium-binding protein
**[[4o27]] – hChk24 kinase domain (mutant) + calcium-binding protein
**[[4qml]] – hChk Mst3 kinase domain + AMPPNP
*'''Chk25 or STK25'''
**[[2xik]] – hChk25 kinase domain
**[[7z4v]] – hChk25 kinase domain + inhibitor
**[[3w8h]] – hChk25 regulatory domain + programmed cell death protein 10
**[[4nzw]] – hChk25 kinase domain (mutant) + calcium-binding protein
*'''Chk26 (Mst4)'''
**[[3ggf]], [[7b36]] – hChk Mst4 + inhibitor
**[[4geh]], [[3w8i]] - hChk Mst4 dimerization domain + programmed cell death protein 10
**[[4fza]], [[4fzd]], [[4fzf]] – hChk Mst4 (mutant) + calcium-binding protein
*'''Chk32'''
**[[4fr4]] – hChk32A
*'''Chk38'''
**[[6bxi]] – hChk38 kinase domain
*'''Chk39''' or SPAK
**[[7o86]] – hChk39 C-terminal
**[[5d9h]] – mChk39 residues 63-403 + ATP
**[[5dbx]] – mChk39 residues 63-403 (mutant) + AMPPNP
*'''Chk40'''
**[[5l2q]] – hChk40 kinase homology domain
*'''Dclk1'''
**[[6kyq]] – hChk Dclk1 kinase domain
**[[6kyr]] – hChk Dclk1 kinase domain (mutant)
**[[5jzj]] – hChk Dclk1 kinase domain + AMPPN
**[[5jzn]], [[7kx6]], [[7kxw]] – hChk Dclk1 kinase domain + inhibitor
**[[7f3g]] – hChk Dclk1 kinase domain + drug
**[[7kx8]] – hChk Dclk1 C-terminal + inhibitor
*'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123; kinase 144-480
**[[1unp]], [[1unr]] – hRac-α hChk pleckstrin homology domain
**[[2uzr]], [[2uzs]], [[7myx]] – hRac-α hChk pleckstrin homology domain (mutant)
**[[1h10]], [[1unq]], [[2uvm]] – hRac-α hChk pleckstrin homology domain + inositol tetrakisphosphate
**[[3o96]], [[4ejn]], [[6s9w]], [[6s9x]], [[6hhj]], [[6hhi]], [[6hhh]], [[6hhg]], [[6hhf]] - hRac-α hChk + inhibitor
**[[5kcv]], [[7nh4]], [[7nh5]] - hRac-α hChk (mutant) + inhibitor
**[[4gv1]], [[4ekl]] - hRac-α hChk kinase domain + inhibitor
**[[3qkm]], [[6ccy]] - hRac-α hChk kinase domain (mutant) + inhibitor
**[[6buu]] - hRac-α hChk kinase domain + bisubstrate peptide
**[[4ekk]] - hRac-α hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[6npz]] - hRac-α hChk kinase domain + peptide + inhibitor
**[[3ow4]], [[3qkk]], [[3qkl]], [[6buu]] - hRac-α hChk kinase domain (mutant) + peptide + inhibitor
**[[7apj]] - hRac-α hChk + nanobody
*'''Rac-β hChk (AKT2)'''
**[[1gzk]], [[1gzn]], [[1gzo]], [[1mrv]], [[1mry]] – hRac-β hChk kinase domain
**[[1p6s]] - hRac-β hChk pleckstrin homology domain - NMR
**[[1o6k]] - hRac-β hChk kinase domain + GSK3 peptide + AMPPNP
**[[2jdo]], [[2jdr]], [[2uw9]], [[2x39]], [[3cqu]], [[3cqw]] - hRac-β hChk kinase domain + GSK3 peptide + inhibitor
**[[3e87]], [[3e88]], [[3e8d]] - Rac-β hChk kinase domain (mutant) + GSK3 peptide + inhibitor<br /
**[[1o6l]] - hRac-β hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[3d0e]], [[8q61]] - hRac-β hChk kinase domain (mutant) + inhibitor
*'''Rac-γ hChk (ATK3)'''
**[[2x18]] – Rac-γ hChk PH domain
*'''A-Raf'''
**[[1wxm]] – hA-Raf RAS-binding domain 19-91 - NMR
**[[2mse]] – hA-Raf RAS-binding domain + APOA-I + K-ras - NMR
*'''B-Raf'''; domains - BRS 38-116; Ras-binding 153-237; kinase 445-723
**[[8dgs]], [[8dgt]] – hB-Raf in Ras/Raf complex – Cryo EM
**[[7z37]], [[7z38]], [[7zr5]] – hB-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
**[[1uwh]], [[3c4c]], [[6v2u]], [[6xfp]], [[6xlo]], [[8f7o]], [[8f7p]] – hB-Raf kinase domain + anticancer drug
**[[1uwj]], [[6p3d]] – hB-Raf kinase domain (mutant) + anticancer drug
**[[2fb8]], [[3d4q]], [[3ii5]], [[3psd]], [[3skc]], [[3tv6]], [[4g9c]], [[4ksp]], [[4ksq]], [[3psb]], [[3ppj]], [[3ppk]], [[3prf]], [[3pri]], [[3tv4]], [[4dbn]], [[4e4x]], [[4mbj]], [[4ehe]], [[3q4c]], [[3q96]], [[3e26]], [[4h58]], [[4e26]], [[4fc0]], [[4pp7]], [[6cad]], [[7shv]] – hB-Raf kinase domain + pyrazole inhibitor
**[[4jvg]], [[4ehg]], [[4fk3]], [[3idp]], [[4g9r]], [[4wo5]], [[4mnf]], [[4r5y]], [[4rzv]], [[4rzw]], [[4xv1]], [[4xv2]], [[4xv3]], [[4xv9]], [[4yht]], [[5c9c]], [[5hi2]], [[5ita]], [[5jrq]], [[5jsm]], [[5jt2]], [[6nsq]], [[6p7d]], [[6uuo]] – hB-Raf kinase domain (mutant) + pyrazole inhibitor
**[[5csw]], [[5csx]], [[5ct7]], [[5fd2]], [[5hid]], [[5hie]], [[5val]], [[5vam]], [[6b8u]], [[6n0q]], [[6n0p]], [[7k0v]], [[7p3b]], [[7p3v]], [[8c7x]], [[8c7y]] - hB-Raf kinase domain + inhibitor
**[[6v34]] – hB-Raf kinase domain (mutant) + inhibitor
**[[4mne]] – hB-Raf kinase domain + MAPKK1
**[[8f7o]] – hB-Raf kinase domain + drug
**[[7m0u]] – hB-Raf kinase domain + AMPPNP + drug
**[[6u2h]] – hB-Raf kinase domain + 14-3-3 ζ/δ
**[[7mfe]] – hB-Raf + 14-3-3 ζ/δ – Cryo EM
**[[7mff]] – hB-Raf + 14-3-3 ζ/δ + inhibitor – Cryo EM
**[[7mfd]] – hB-Raf + 14-3-3 ζ/δ + MEK + inhibitor – Cryo EM
**[[6pp9]] – hB-Raf kinase domain + MEK1 + ANP
**[[7m0x]], [[7m0z]] – hB-Raf kinase domain + MEK1 + ANP + inhibitor
**[[7m0t]], [[7m0u]], [[7m0v]], [[7m0w]], [[7m0y]] – hB-Raf kinase domain + MEK1 + ANP + drug
**[[6u2g]] – hB-Raf kinase domain + MEK1 + AMPPCP
**[[5vr3]] – hB-Raf BRS domain
**[[7jhp]] – hB-Raf BRS domain + Hras
**[[6ntc]], [[6ntd]] – hB-Raf BRS domain (mutant) + Hras
**[[6xi7]] – hB-Raf 52-188 + Kras
**[[2l05]], [[5j17]], [[5j2r]] – hB-Raf RAS-binding domain - NMR
**[[3ny5]] – hB-Raf RAS-binding domain
**[[5j18]] – hB-Raf RAS-binding domain + inhibitor - NMR
**[[6pts]], [[6ptw]] – hB-Raf 56-187 + Kras + apolipoprotein + GMPPNP - NMR
**[[6uan]], [[6q0k]] – hB-Raf + 14-3-3 ζ – Cryo EM
**[[6nyb]] – hB-Raf + 14-3-3 ζ + MEK1 – Cryo EM
**[[6q0t]], [[6q0j]] – hB-Raf (mutant) + 14-3-3 ζ + MEK1 – Cryo EM
*'''c-Raf'''; Domains – RAS-binding (RBD) 55-132; Cys-rich 136-187 (CBD); kinase 323-618
**[[1rfa]], [[8jna]], [[8jof]], [[8jog]] – hc-Raf RBD - NMR
**[[1faq]], [[1far]] – hc-Raf cysteine-rich domain - NMR
**[[3omv]] – hc-Raf kinase domain
**[[1rrb]] – c-Raf RBD – NMR - rat
*c-Raf complex with protein
**[[8cpd]] – hc-Raf + 14-3-3 protein zeta – Cryo EM
**[[9mmp]] – hc-Raf + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[9mmr]] – hc-Raf (mutant) + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[1c1y]] – hc-Raf RBD + RAP1A
**[[3kuc]] – hc-Raf RBD (mutant) + RAP1A
**[[1gua]] – hc-Raf RBD + RAP1A + GPPNHP
**[[8jnb]] – hc-Raf RBD + ligand
**[[4g0n]], [[4g3x]] – hc-Raf RBD + GTPase Hras
**[[3kud]] – hc-Raf RBD (mutant) + GTPase Hras
**[[8epw]], [[8t74]] – hc-Raf RBD + GTPase K-ras
**[[8t75]], [[9ygs]] – hc-Raf RBD-CRD + GTPase K-ras + GMPPNP
**[[9ay7]], [[9aya]] – hc-Raf + MEK1
**[[9mmq]] – hc-Raf + MEK1 – Cryo EM
**[[9mms]] – hc-Raf (mutant) + MEK1 – Cryo EM
**[[9o0u]], [[9o0v]] – hc-Raf (mutant) + MEK1 + ANP + inhibitor– Cryo EM
**[[8u1l]] – hc-Raf + Hsp90 + CDC37 – Cryo EM
**[[8gae]], [[8gft]] – hc-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
*'''Snf1-related Chk'''
**[[3uc4]], [[3uc3]], [[3udb]], [[3zut]], [[3zuu]] – AtChk Srk2E kinase domain (mutant) – ''Arabidopsis thaliana''
**[[3ujg]] – AtChk Srk2E kinase domain (mutant) + protein phosphatase 2C
**[[5yks]] – hChk
*'''MAPK-interacting Chk''' or Mnk1 Mnk2
**[[2hw6]] – hMnk 1 catalytic domain
**[[2hw7]] – hMnk 1 catalytic domain + staurosporin
**[[5wvd]] – hMnk 1 catalytic domain + inhibitor
**[[2ac3]] – hMnk 2 catalytic domain
**[[2ac5]] – hMnk 2 catalytic domain (mutant)
**[[6cj5]], [[6cje]], [[6cjh]], [[6cjw]], [[6cjy]], [[6ck3]], [[6ck6]], [[6cki]] – hMnk 2 catalytic domain (mutant) + inhibitor
*'''hChk Pak''' or '''Chk N''' or '''PRK1'''; Domains - CRIB 74-109; Hr1B 122-199; catalytic 109-426; kinase 605-942
**[[1urf]] – hChk Pak-1 Hr1b domain - NMR
**[[4nkg]] – hChk Pak-1 Hr1b domain + SSPH1 LRR domain
**[[2rmk]] – hChk Pak-1 Hr1bb domain + Rac1 - NMR
**[[1f3m]] – hChk Pak-1 autoregulatory+kinase domains
**[[4otd]] - hChk Pak-1 kinase domain
**[[1yhv]], [[1yhw]], [[3q4z]], [[3q52]], [[3q53]] – hChk Pak-1 kinase domain (mutant)
**[[4o0r]], [[4o0t]], [[4zji]], [[4zjj]], [[4zlo]], [[4zy4]], [[4zy5]], [[4zy7]], [[5ime]], [[5kbq]], [[5kbr]], [[6b16]], [[7vto]] – hChk Pak-1 kinase domain + inhibitor
**[[4oti]], [[4oth]], [[4otg]] – hChk Pak-1 kinase domain + inhibitor
**[[4eqc]], [[4p90]], [[5dew]], [[5dey]], [[5dfp]] – hChk Pak-1 kinase domain (mutant) + inhibitor
**[[2hy8]] – hChk Pak-1 kinase domain + staurosporin
**[[2qme]] – hChk Pak-1 CRIB domain + RAC3
**[[3fxz]], [[3fy0]], [[4daw]] – hChk Pak-1 kinase domain (mutant) + Ru complex
**[[6fd3]] – hChk Pak-3 kinase domain (mutant)
**[[2j0i]], [[4fie]] – hChk Pak-4
**[[4fig]], [[4fij]], [[4l67]] – hChk Pak-4 kinase domain
**[[2cdz]] – hChk Pak-4 + purine derivative
**[[2ov2]] – hChk Pak-4 CRIB domain + RAC3
**[[2qon]], [[4fif]], [[4fih]], [[4fii]], [[4jdh]], [[4jdi]], [[4jdj]], [[4jdk]], [[6wlx]], [[6wly]] – hChk Pak-4 kinase domain + peptide
**[[4app]], [[4o0v]], [[4o0x]], [[4o0y]], [[4njd]], [[4xbu]], [[5bms]], [[5i0b]], [[5vee]], [[5vef]], [[5zjw]], [[5xvg]], [[5xvf]], [[5xva]], [[7cmb]], [[7cp3]], [[7cp4]] – hChk Pak-4 kinase domain + inhibitor
**[[2x4z]], [[2xh5]] – hChk Pak-4 kinase domain (mutant) + inhibitor
**[[5upl]], [[5upk]] – hChk Pak-4 kinase domain (mutant) + CDC42
**[[5ved]] – hChk Pak-4 kinase domain + staurosporine
**[[8ahi]] – hChk Pak-4 300-591 + inhibitor
**[[7s46]], [[7s48]] – hChk Pak-4 catalytic domain + integrin beta-5 peptide
**[[2c30]] – hChk Pak-6
**[[2odb]] – hChk Pak-6 CRIB domain + CDC42
**[[4ks8]] – hChk Pak-6 kinase domain + sunitinib
**[[4ks7]] – hChk Pak-6 kinase domain (mutant) + inhibitor
**[[2f57]] – hChk Pak-7
*'''Mycobacterium tuberculosis Chk Pkn'''
**[[4x3f]] - MtChk PknA – ''Mycobacterium tuberculosis''
**[[4ow8]] - MtChk PknA kinase domain
**[[3ori]], [[3ork]], [[3orl]], [[3orm]], [[3oro]], [[3orp]], [[3ort]] - MtChk PknB kinase domain (mutant)
**[[1o6y]] – MtChk PknB kinase domain
**[[6b2p]], [[6b2q]] – MtChk PknB kinase domain + inhibitor
**[[2kud]], [[2kue]], [[2kuf]], [[2kui]] – MtChk PknB pasta domains 2-3 - NMR
**[[3ouv]] – MtChk PknB pasta domain 3
**[[5e0y]] – MtChk PknB pasta domain 4
**[[5e10]] – MtChk PknB pasta domains 1-2
**[[5e0z]] – MtChk PknB pasta domains 3-4
**[[5e12]] – MtChk PknB pasta domains 2-4
**[[5u94]] - MtChk PknB kinase domain + inhibitor
**[[3f61]], [[3f69]] - MtChk PknB kinase domain (mutant) + inhibitor
**[[6i2p]] - MtChk PknB kinase domain (mutant) + GARA + peptide
**[[1rwi]], [[1rwl]] - MtChk PknD extracellular domain
**[[2h34]] – MtChk PknE catalytic domain
**[[7naa]] – MtChk PknF kinase domain + inhibitor
**[[4y12]] - MtChk PknG + ATP-gS
**[[4y0x]] - MtChk PknG + ADP
**[[7q52]] - MtChk PknG + inhibitor
**[[4esq]] - MtChk PknH extracellular domain
**[[5m06]], [[5xka]] - MtChk PknI kinase domain
**[[5m07]], [[5m08]], [[5m09]] - MtChk PknI kinase domain (mutant)
**[[5xlm]], [[5xll]] - MtChk PknI sensor domain
**[[7mxb]], [[7mxj]], [[7mxk]] - Chk PknG kinase domain + AMPPNP - Corynebacterium glutamicum
*'''hChk Nek'''
**[[4apc]] – hChk Nek1 kinase domain (mutant)
**[[4b9d]] - hChk Nek1 kinase domain (mutant) + inhibitor
**[[2w5h]] – hChk Nek2 kinase domain
**[[2jav]], [[2wqo]], [[2xk3]], [[2xk4]], [[2xk6]], [[2xk7]], [[2xk8]], [[2xkc]], [[2xkd]], [[2xke]], [[2xkf]], [[2xnm]], [[2xnn]], [[2xno]], [[2xnp]], [[4a4x]], [[4afe]], [[5m51]], [[5m53]], [[5m55]], [[5m57]], [[6sgd]], [[6sgh]], [[6sgi]], [[6sgk]], [[6sk9]] – hChk Nek2 + inhibitor
**[[2w5a]], [[2w5b]] – hChk Nek2 + nucleotide
**[[6tm5]] - hChk Nek2 in anaphase-promoting complex – Cryo EM
**[[2wqm]], [[6s76]] – hChk Nek7
**[[2wqn]] – hChk Nek7 + ADP
**[[5de2]] – hChk Nek7 + hChk Nek9
**[[6s73]], [[2wqo]] – hChk Nek7 + inhibitor
**[[6npy]] – hChk Nek7 + Nlrp3
**[[6s75]] – hChk Nek7 + inhibitor
*'''Chk Rio'''
**[[6fdo]], [[6fdn]], [[6fdm]] – hChk Rio2
**[[4otp]] – hChk Rio1 Rio domain + ADP
**[[6hk6]], [[7vbt]] – hChk Rio2 + inhibitor
**[[6eml]], [[6fai]], [[6g18]], [[6g51]], [[6rbd]],[[6rbe]], [[6y7c]] – yChk Rio2 in 40S particle – Cryo EM
**[[1ztf]] – AfChk Rio1 + adenine derivative – Archaeoglobus fulgidus
**[[1zth]] – AfChk Rio1 + ADP
**[[1zp9]] – AfChk Rio1 + ATP
**[[1tqp]], [[1zao]] – AfChk Rio2 + ATP
**[[1zar]] – AfChk Rio2 + ADP
**[[4gyg]] – CtChk Rio2 – Chaetonium thermophilum
**[[4gyi]] – CtChk Rio2 + ADP
*hChk Vrk (vaccinia-related kinase)
**[[2kty]], [[2kul]], [[2lav]], [[2rsv]] – hChk Vrk1 kinase domain 1-396 - NMR
**[[3op5]] – hChk Vrk1 kinase domain (mutant)
**[[5ukf]] – hChk Vrk1 kinase domain + inhibitor
**[[5uvf]], [[6cnx]], [[6bu6]], [[6cfm]], [[6dd4]], [[6bp0]], [[6bru]], [[6btw]], [[6cmm]], [[6cqh]], [[6csw]], [[6npn]], [[6vxu]], [[6vzh]] – hChk Vrk1 kinase domain (mutant) + inhibitor
**[[6ac9]] – hChk Vrk1 kinase domain (mutant) + AMPPNP
**[[7tan]] – hChk Vrk1 kinase domain + nucleosome – Cryo EM
**[[2v62]] – hChk Vrk2 kinase domain
**[[5uu1]], [[6ncg]], [[8q1z]] – hChk Vrk2 kinase domain + inhibitor
*Chk Wnk (protein kinase lysine-deficient); Domains - kinase 194-483; CCT1 454-549
**[[6cn9]], [[4q2a]], [[4pwn]] - hChk Wnk1 kinase domain (mutant)
**[[5tf9]] - hChk Wnk1 kinase domain + inhibitor + AMPPNP
**[[5wdy]], [[5we8]] - hChk Wnk1 kinase domain + inhibitor + ANP
**[[5drb]], [[6ol2]]- rChk Wnk1 kinase domain (mutant) + inhibitor
**[[6elm]] - hChk Wnk2 CCT1 domain
**[[6fbk]] - hChk Wnk2 CCT1 domain + Wnk1 peptide
**[[5o1v]], [[5o21]], [[5o23]] - hChk Wnk3 kinase domain
**[[5o2c]] - hChk Wnk3 kinase + CCT1 domains
**[[5o26]], [[5tf9]] - hChk Wnk3 kinase domain + AMPPNP
**[[5o2b]] - hChk Wnk3 kinase domain + inhibitor
**[[8edh]] - hChk Wnk3 kinase domain (mutant) + inhibitor
**[[2lru]] – rChk Wnk1 autoinhibitory domain 480-572 - NMR
**[[5w7t]] - rChk Wnk1 kinase domain
**[[7uos]] - rChk Wnk1 kinase domain (mutant)
*'''TANK-binding kinase'''
**[[4efo]] – hChk Tbk1 ubiquitin-like domain
**[[6rsr]], [[6rsu]] – hChk Tbk1 + inhibitor
**[[4im0]], [[4im2]], [[4im3]], [[4iw0]], [[4iwo]], [[4iwp]], [[4ipq]], [[6rst]] – hChk Tbk1 (mutant) + inhibitor
**[[6cq5]], [[6cq4]], [[6cq0]], [[6boe]], [[6bod]], [[6bny]], [[5w5v]] – hChk Tbk1 + ulcer drug
**[[4eut]], [[4euu]] – hChk Tbk1 kinase+ubiquitin-like domains (mutant) + inhibitor
**[[6nt9]] – hChk Tbk1 (mutant) + STING
**[[5eoa]], [[5eof]] – hChk Tbk1 residues 677-729 + optineurin
**[[4jl9]], [[4jlc]] – mChk Tbk1 + inhibitor
**[[6o8c]], [[6o8b]] – mChk Tbk1 (mutant) + STING
*'''Haspin'''
**[[2vuw]], [[2wb8]] – hChk Haspin kinase domain
**[[3dle]] – hChk Haspin kinase domain + AMP
**[[3e7v]], [[3f2n]], [[3fmd]], [[3iq7]], [[4qtc]], [[5htb]], [[5htc]], [[6z56]], [[6z57]], [[6z58]], [[6z59]], [[6z5a]], [[6z5b]], [[6z5c]]. [[6z5d]], [[6z5e]] , [[7avq]], [[7ops]] – hChk Haspin kinase domain + inhibitor
**[[7sqm]] – hChk Haspin kinase domain + antimalarial
**[[6g38]], [[6g34]], [[6g35]], [[6g36]], [[6g37]] – hChk Haspin kinase domain + tubercidin derivative
**[[6g39]], [[6g3a]] – hChk Haspin kinase domain (mutant) + tubercidin derivative
**[[4ouc]] – hChk Haspin kinase domain + histone H3 peptide
*'''MAP/microtubule affinity-regulating kinase (MARK)'''
**[[2hak]] – hChk MARK1 catalytic+UBA domains
**[[3ose]] - hChk MARK1 KA1 domain
**[[6c9d]] – hChk MARK1 catalytic+UBA+KA1 domains (mutant)
**[[5eak]], [[5kz7]], [[5kz8]] – hChk MARK2 catalytic+UBA domains + inhibitor
**[[3iec]] – hChk MARK2 catalytic+UBA domains + cytotoxicity-associated immunodominant antigen peptide
**[[2qnj]] – hChk MARK3 catalytic+UBA domains
**[[3fe3]] – hChk MARK3 catalytic+UBA domains (mutant)
**[[7p1l]] – hChk MARK3 catalytic+UBA domains + inhibitor
**[[5es1]] – hChk MARK4 catalytic+UBA domains + inhibitor
**[[1zmu]] – rChk MARK2 catalytic+UBA domains
**[[2wzj]], [[2r0i]], [[1zmv]], [[1y8g]], [[1zmw]] – rChk MARK2 catalytic+UBA domains (mutant)
**[[1ul7]], [[1v5s]] - mChk MARK3 catalytic domain - NMR
*'''Mitotic checkpoint Chk (Bub)'''; Domains: TPR 1-220; kinase 726-1085
**[[2lah]] – hChk Bub1 TPR domain – NMR
**[[2wvi]] – hChk Bub1β TPR domain
**[[3si5]] – hChk Bub1 TPR domain + CASC5 peptide
**[[4r8q]], [[4qpm]], [[5dmz]] – hChk Bub1 kinase domain + ADP
**[[6f7b]] – hChk Bub1 kinase domain + inhibitor
**[[4a1g]] – hChk Bub1 TPR domain + CASC5 KI motif
**[[4ggd]] - hChk Bub1 + cell division cycle protein
**[[6tlj]], [[5khu]] - hChk Bub1 in anaphase-promoting complex – Cryo EM
**[[6jkk]] – DmChk Bub1 kinase domain
**[[6jkm]] – DmChk Bub1 kinase domain + ADP
**[[5jja]] – hChk Bub1 residues 661-734 + PP2A
**[[3esl]] – yChk Bub1 N terminal
**[[4bl0]] - yChk Bub1 + cell cycle arrest protein Bub3
*'''Microtubule-associated Chk'''
**[[2m9x]] – hChk 1 residues 187-287 – NMR
**[[3ps4]] - hChk 1 residues 965-1057
**[[2kqf]], [[2kyl]] – hChk 2 PDZ domain + glycoprotein C terminal – NMR
**[[3khf]] - hChk 3 PDZ domain
**[[2w7r]] – hChk 4 PDZ domain
*'''mTOR''' or '''Mechanistic target of rapamycin'''
*''mTOR FRB domain residues 2015-2114''
**[[1nsg]], [[1fap]] – hFRAP FRB domain + FKBP
**[[2rse]] – hFRAP FRB domain + FKBP – NMR
**[[1aue]] – hFRAP FRB domain
**[[2gaq]], [[2npu]] – hFRAP FRB domain - NMR
**[[8ppz]] – hFRAP FRB domain + FKBP + pyridine derivative
**[[3fap]], [[2fap]], [[4fap]] – hFRAP FRB domain + FKBP + rapamycin analog
**[[4drh]], [[4dri]], [[4drj]], [[5gpg]] – hFRAP FRB domain + FKBP + rapamycin
**[[6m4u]], [[6m4w]] – hChk Mtor FRB domain (mutant) + FKBP1A + rapamycin
**[[5wbh]] – hFRAP FRB domain + S6K1 peptide
*''mTOR FAT+PIKK domain residues 1376-2549''
**[[4jsn]] – hFRAP + TORC subunit LST8
**[[4jsp]] – hFRAP + TORC subunit LST8 + ATP
**[[4jsv]] – hFRAP + TORC subunit LST8 + ADP
**[[4jsx]] – hFRAP + TORC subunit LST8 + torin2
**[[4jt5]] – hFRAP + TORC subunit LST8 + pp242
**[[4jt6]] – hFRAP + TORC subunit LST8 + PI-103
**[[5wby]], [[5wbu]] – hFRAP + TORC subunit LST8 + proline-rich Akt1 substrate
*''mTOR complex''
**[[5flc]] – hmTOR + RAPTOR + LST8 + FKBP – Cryo EM
**[[5h64]] – hmTOR + RAPTOR + LST8 – Cryo EM
**[[6sb2]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC – Cryo EM
**[[6sb0]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC + proline-rich Akt1 substrate – Cryo EM
**[[5zcs]] – hmTOR + LST8 + AVO3 + TORC2 – Cryo EM
**[[7tzo]] – hTORC2 in mTORC2 complex– Cryo EM
**[[6zwm]], [[6zwo]], [[7owg]], [[7pe7]], [[7pe8]], [[7pe9]], [[7pea]], [[7peb]], [[7pec]], [[7uxc]] , [[8era]]– mTOR in mTor complex – Cryo EM
*'''Gcn2'''
**[[1zyc]] – yChk Gcn2
**[[1zxe]], [[1zy4]], [[1zy5]] – yChk Gcn2 (mutant)
**[[2yz0]] – yChk Gcn2 RWD/GI domain – NMR
**[[4otm]] – yChk Gcn2 C terminal domain
**[[1zyd]] – yChk Gcn2 + ATP
**[[4otn]] – mChk Gcn2 C terminal domain
*'''LRRK1''' or leucine-rich repeat Chk1
**[[8e04]], [[8e05]], [[8e06]], [[8fac]] – hLRRK1 – Cryo EM
*'''LRRK2''' or leucine-rich repeat Chk2 or dardarin
**[[6xr4]] – hLRRK2 – Cryo EM
**[[7lht]], [[7lhw]], [[7li4]] – hLRRK2 + ATP + GDP – Cryo EM
**[[7li3]] – hLRRK2 (mutant) + ATP + GDP – Cryo EM
**[[6oje]], [[7thy]] – hLRRK2 GTPase domain 1329-1520
**[[6ojf]] – hLRRK2 GTPase domain (mutant)
**[[6dlo]], [[6dlp]] – hLRRK2 WD40 domain
**[[7thz]] – hLRRK2 1330-1527 + GDP
**[[6vno]], [[6vp6]], [[6vp7]] – hLRRK2 C terminal 1330-2527 – Cryo EM
**[[6vp8]] – hLRRK2 C terminal 1330-2527 + COR domain 1670-1950 + WD40 domain 2140-2489 – Cryo EM
**[[6s6q]] – AtLRRK2 ectodomain + protein casparian strip peptide
*'''Pim'''
*Pim1 catalytic domain residues 14-313
**[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain
**[[1yxs]] – hPim1 catalytic domain (mutant)
**[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP
**[[1yxu]] – hPim1 catalytic domain + AMP
**[[1yxv]], [[5ipj]] – hPim1 catalytic domain + quinoline derivative
**[[1yxx]] – hPim1 catalytic domain + indole derivative
**[[2bzh]], [[2bzi]], [[2bzj]] – hPim1 catalytic domain (mutant) + organometallic ligand
**[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3c4e]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umw]], [[3umx]], [[4enx]], [[4eny]], [[4k1b]], [[4k18]], [[4k0y]], [[4iaa]], [[4i41]], [[4ll5]], [[4lm5]], [[4lmu]], [[4mta]], [[4med]], [[4mbl]], [[4mbi]], [[4n6y]], [[4n6z]], [[4n70]], [[4xh6]], [[5iis]], [[5kgd]], [[5kge]], [[5kgg]], [[5kgi]], [[5kgk]], [[5kzi]], [[5vua]], [[5vub]], [[5vuc]], [[6mt0]], [[6vrv]], [[7oov]], [[7oow]], [[7oox]], [[7xsv]] – hPim1 catalytic domain + inhibitor
**[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor
*Pim1 kinase domain residues 92-404
**[[4jx3]] – hPim1 kinase domain
**[[3uix]], [[5c1q]] – hPim1 kinase domain residues 120-404 + quinoline derivative
**[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate
**[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand
**[[1xws]], [[4alu]], [[4alv]], [[4alw]], [[4as0]], [[4bzn]], [[4bzo]], [[4dtk]], [[4jx7]], [[4rbl]], [[4rc2]], [[4rc3]], [[4rc4]], [[4ty1]], [[4wrs]], [[4wsy]], [[4wt6]], [[4xhk]], [[5dgz]], [[5dhj]], [[5dia]], [[5dwr]], [[5eol]], [[5kcx]], [[5o11]], [[5o12]], [[5o13]], [[5tel]], [[5tex]], [[5toe]], [[5v80]], [[5v82]]. [[6bsk]], [[6kzi]], [[6l11]], [[6l12]], [[6l13]], [[6l14]], [[6l15]], [[6l16]], [[6l17]], [[6no8]], [[6no9]], [[6vru]], [[6ykd]], [[7zun]] – hPim1 kinase domain + inhibitor
**[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor
*Pim1 full length
**[[4rpv]], [[5tur]] - hPim1 + inhibitor
*Pim1 complex with consensus peptide (pimtide)
**[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6qxk]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]] – hPim1 kinase domain + inhibitor + consensus peptide
**[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide
**[[2c3i]], [[5ndt]], [[5n5m]], [[5n5l]], [[5n52]], [[5n51]], [[5n50]], [[5n4z]], [[5n4y]], [[5n4x]], [[5n4v]], [[5n4u]], [[5n4r]], [[5n4o]], [[5n4n]], [[5mzl]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide
**[[4gw8]], [[7qb2]], [[7qfm]], [[7z6u]], [[8afr]] – hPim1 catalytic domain (mutant) + inhibitor + pimtide
**[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide
**[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide
*Pim1 containing phosphorylated Ser 261
**[[1yhs]] – hPim1 kinase domain + PSer + staurosporine
**[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor
**[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor
**[[1yi4]] – hPim1 kinase domain + PSer + adenosine
*Pim2
**[[4x7q]] – hPim2 catalytic domain + inhibitor
**[[2iwi]] – hPim2 catalytic domain + Ru ligand
*'''Rip or receptor-interacting Chk; Domains – catalytic 1-294; Amyloid fibril 418-518; Death 561-671'''
**[[6ac5]] – hRip1 death domain
**[[6r5f]], [[6nw2]], [[6c4d]], [[6c3e]], [[5tx5]], [[7fcz]], [[7fd0]], [[7ydx]] – hRip1 catalytic domain + inhibitor
**[[6rln]], [[6ocq]], [[6nyh]], [[6hho]] – hRip1 catalytic domain (mutant) + inhibitor
**[[6ggs]] – hRip2 – Cryo EM
**[[5yrn]] – hRip2 CARD domain 434-540 – Cryo EM
**[[6szj]], [[6sze]], [[6s1f]], [[6rna]], [[6rn8]], [[6hmx]], [[6fu5]], [[6es0]], [[5w5o]], [[5w5j]] – hRip2 catalytic domain + inhibitor
**[[6ul8]] – hRip2 catalytic domain (mutant) + inhibitor
**[[8aza]] – hRip2 catalytic domain + XiaP Bir2 domain – Cryo EM
**[[7mx3]] – hRip3 catalytic domain (mutant) + inhibitor
**[[7mon]] – hRip3 catalytic domain (mutant) + MLKL
**[[7dac]] – hRip3 amyloid fibril - NMR
**[[7da4]] – hRip3 amyloid fibril – Cryo EM
**[[6oko]] – mRip3 catalytic domain + inhibitor
**[[6jpd]] – mRip3 residues 409-486 - NMR
**[[5wnm]], [[5wnj]] – mRip4 catalytic domain (mutant) + drug
**[[5wnl]] – mRip4 catalytic domain (mutant) + staurosporine
**[[5wnk]] – mRip4 catalytic domain (mutant) + inhibitor
**[[5wni]] – mRip4 catalytic domain (mutant) + ATP
**[[6gwm]] – rRip2 caspase recruitment domain 433-539
*'''Ulk'''
**[[6qas]] – hChk Ulk1 + inhibitor
**[[5ci7]], [[6mnh]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[8soi]], [[8sqz]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein
**[[8srm]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein – Cryo EM
**[[8srq]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein + PI3K – Cryo EM
**[[6qav]], [[6qau]], [[6qat]], [[6yid]] – hChk Ulk2 + inhibitor
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[6fdz]], [[6fdy]] – hChk Ulk3 + leukemia drug
**[[6tsz]] – hChk Ulk4 pseudfokinase domain + ATPgS
**[[6u5l]] – hChk Ulk4 (mutant) + inhibitor
*'''Hipa''' and '''Hipb'''
**[[3tpd]], [[3tpe]] – EcChk Hipa – ''Escherichia coli''
**[[3tpb]], [[3dnt]], [[3dnu]] – EcChk Hipa (mutant)
**[[4pu7]], [[4pu8]] – SoChk Hipb - ''Shewanella oneidensis''
**[[3tpt]] – EcChk Hipa (mutant) + ADP
**[[3fbr]] – EcChk Hipa (mutant) + AMPPNP + peptide
**[[3tpv]] – EcChk Hipa + ADP
**[[2wiu]] – EcChk Hipa + Hipb
**[[4yg7]], [[5k98]], [[3hzi]], [[3dnv]] – EcChk Hipa + Hipb + DNA
**[[4yg1]], [[4z58]], [[4z59]], [[4z5c]], [[4z5d]] – EcChk Hipb + DNA
**[[4z5h]] – EcChk Hipb (mutant) + DNA
**[[4pu3]], [[4pu4]] – SoChk Hipa + Hipb + DNA - ''Shewanella oneidensis''
**[[4pu5]] – SoChk Hipa + AMPPNP
*'''Chk Smg'''
**[[6l53]] – hChk Smg1 – Cryo EM
**[[7pw6]] – hChk Smg1 + inhibitor – Cryo EM
**[[7pw7]] – hChk Smg1 + Smg9 + inhibitor – Cryo EM
**[[7pw9]] – hChk Smg1 + Smg9 + AMPPNP + ATP – Cryo EM
**[[6l54]], [[6syt]] – hChk Smg1 + Smg8 + Smg9 – Cryo EM
**[[7pw4]], [[7pw5]] – hChk Smg1 + Smg8 + Smg9 + inhibitor – Cryo EM
**[[7pw8]] – hChk Smg1 + Smg8 + Smg9 + AMPPNP – Cryo EM
**[[6z3r]] – hChk Smg1 + Smg8 + Smg9 + regulator of nonsense transcripts – Cryo EM
**[[2hwy]] – hChk Smg5 PIN domain
**[[2hww]], [[2hwx]] – hChk Smg6 PIN domain (mutant)
**[[4um2]] – hChk Smg6 TPR domain
**[[1ya0]] – hChk Smg7 N terminal
*'''Chk Vprbp or DCAF1'''
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain 1039-1401 (mutant)
**[[7sse]], [[7ufv]], [[8f8e]], [[8og5]], [[8og6]], [[8og7]], [[8og8]], [[8og9]], [[8oga]], [[8ogb]], [[8ogc]], [[8oo5]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) + inhibitor
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[5aja]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
*'''Other Chk'''
**[[1wak]] – hChk Sprk1
**[[3dak]] – hChk Osr1 kinase domain
**[[7okw]] – hChk Osr1 C-terminal
**[[4aw2]] – hChk Mrckα kinase domain
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain (mutant)
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[1uf0]] – hChk Dcamkl1 DCX domain – NMR
**[[1u5q]] – rChk Tao2 kinase domain
**[[2cos]] – mChk Lats2 – NMR
**[[1xte]], [[1xtn]], [[6edx]] – mChk Sgk3 PX domain
**[[4yom]] – mChk Brsk2
**[[4ynz]] – mChk Brsk1 N terminal domain
**[[5iri]] – mChk Brsk1 residues 592-719
**[[5oat]], [[7mp8]] – rfbChk Pink1– red flour beetle
**[[7t3x]] – Chk Pink1 (mutant) – louse
**[[4f0g]] – smChk Roco4 kinase domain – slime mold
**[[5tos]] – AtChk Bik1
**[[1q8z]], [[1zyc]] – yChk
**[[1how]], [[1zxe]], [[1zy4]] – yChk (mutant)
**[[1ow5]], [[1x9x]] – yChk Ste11 SAM domain – NMR
**[[2kio]], [[2kit]], [[1w1n]] – yChk Tor1 FATC domain – NMR
**[[3gre]] – yChk Vps15 WD repeat domain
**[[3osm]], [[3ost]] - yChk Kcc4 kinase domain
**[[5yyx]] – yChk Mek1 FHA domain
**[[6jxc]], [[6jxa]] – yChk Tel1 – Cryo EM
**[[6u69]] – CaChk Yck2 – ''Candida albicans''
**[[6sl1]], [[6sl0]], [[6skz]], [[6sky]] – Chk Tel1 – ''Chaetonium thermophilum'' – Cryo EM
**[[6ra0]] – CeChk Dkf1 – ''Chaenorhabditis elegans''
**[[7z6e]] – CeChk Mrck1 regulatory domain
**[[6tlb]] – Chk – ''Plasmodium falciparum''
*Other Chk complexes
**[[1wbp]], [[7dd1]] – hChk Sprk1 + peptide
**[[3beg]] – hChk Srpk1 + splicing factor SF2
**[[3hdm]], [[3hdn]], [[7pue]] – hChk Sgk1 (mutant) + inhibitor
**[[2r5t]] – hChk Sgk3 + AMPPNP
**[[4yff]], [[4yfi]], [[6b5j]], [[7mgj]], [[7mgk]] – hChk Tnni3k + inhibitor
**[[2v3s]] – hChk Osr1 + hChk Wnk4 peptide
**[[2vwi]] – hChk Osr1 kinase domain + ANP
**[[7que]], [[7quf]] – hChk Drak1 kinase domain + inhibitor
**[[4crs]] – hChk N2 kinase domain + ATPγS
**[[3tku]], [[4ual]], [[3qfv]], [[5ote]], [[5otf]] – hChk Mrckβ + inhibitor
**[[4uak]] – hChk Mrckβ + ADP
**[[5aja]], [[4z8l]], [[4cc9]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
**[[5jk7]] – hChk Vprbp WD repeat domain + VPX + DDB1 + UDG
**[[3wa0]], [[4p7i]] – hChk Vprbp residues 1417-1506 + merlin
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[5ci7]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[5b5w]], [[5b6b]], [[5brk]] – hChk Lats1 residues 622-704 + MOB1
**[[5yz0]] – hChk Atr + Atr-interacting protein – Cryo EM
**[[6bdn]] – hChk Tao3 kinase domain + ADP
**[[5yh3]] – hChk Fam20C 141-578 + pseudokinase Fam20A
**[[2gcd]] – rChk Tao2 kinase domain + staurosporine
**[[1u5r]] – rChk Tao2 kinase domain + ATP
**[[5yj9]], [[7mp9]] – rfbChk Pink1 kinase domain + AMPPNP
**[[6bn1]] – DmChk Hippo SARAH domain + Shar-Pei
**[[3hgk]] – Chk Pto + effector protein AVRPTOB – Currant tomato
**[[3p86]], [[3ppz]] - AtChk Ctr1 + staurosporine
**[[4f0f]] – smChk Roco4 kinase domain + APPCP
**[[4f1m]], [[4f1o]] – smChk Roco4 kinase domain (mutant) + APPCP
**[[4f1t]], [[4yzm]], [[4yzn]] – smChk Roco4 kinase domain + inhibitor
**[[5fvm]] - Tor2 + LST8 - ''Kluyveromyces marxianus''
**[[5kc2]] - yVps15 + Vps34 - Cryo EM
**[[5dfz]] - yVps15 + Vps34 + Vps30 + VPSAP28 + VPSAP30 - Cryo EM
**[[1q8y]], [[1q97]], [[1q99]], [[1zyd]] – yChk + nucleotide
**[[1zy5]] – yChk (mutant) + nucleotide
**[[2jd5]] – yChk + NPL-3P
**[[4lqs]], [[4lqq]], [[4lqp]] – yChk Cbk1 residues 251-756 + Cbk1 activator Mob2
**[[6emk]] – yChk Tor2 + LST8 + TSC11 + AVO1 + AVO2 – Cryo EM
**[[6s8f]] – yChk Tel1 + AMPPNP – Cryo EM
**[[5yyz]] – yChk Mek1 FHA domain + Hop1
**[[5x6o]], [[6z3a]], [[7wzr]], [[7wzw]]– yChk Mec1 + LCD1 – Cryo EM
**[[6z2w]], [[6z2x]] – yChk Mec1 (mutant) + LCD1 – Cryo EM
**[[7kue]] – yChk Kin28 in TFIIK complex – Cryo EM
**[[6u6a]] – CaChk Yck2 + inhibitor
**[[5fvm]] – Chk Tor2 + LST8 – ''Kluyveromyces maximanus''
*Serine/threonine protein kinase Rad53 see [[Rad53]]
*Serine/threonine protein kinase Gsk3B see [[Glycogen synthase kinase 3]]
}}
[[Category:Topic Page]]

Serine/threonine protein kinase 3D structures

2026-08-19T07:21:33Z

Michal Harel:

==3D structures of serine/threonine protein kinase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Chk1'''; domains - kinase 1-289; KA1 393-492
**[[1ia8]] – hChk1 kinase domain – human
**[[5w12]] – hChk1 KA1 domain
**[[1zlt]] – hChk1 kinase domain + hymenaldisine
**[[1nvq]], [[1nvr]] – hChk1 kinase domain + peptide + saurosporine
**[[1nvs]], [[1zys]], [[7ako]] - hChk1 kinase domain + peptide + inhibitor
**[[7akm]] - hChk1 kinase domain + ATP
**[[2ayp]], [[2br1]], [[2brb]], [[2brg]], [[2brh]], [[2brm]], [[2brn]], [[2bro]], [[2c3j]], [[2c3k]], [[2c3l]], [[2cgu]], [[2cgv]], [[2cgw]], [[2cgx]], [[2e9n]], [[2e9o]], [[2e9p]], [[2e9u]], [[2e9v]], [[2gdo]], [[2ghg]], [[2hog]], [[2hxl]], [[2hxq]], [[2hy0]], [[2qhm]], [[2qhn]], [[2r0u]], [[3f9n]], [[2wmq]], [[2wmr]], [[2wms]], [[2wmt]], [[2wmu]], [[2wmv]], [[2wmw]], [[2wmx]], [[2xey]], [[2xf0]], [[2xez]], [[2x8d]], [[2x8e]], [[2x8i]], [[2ydi]], [[2ydj]], [[2ydk]], [[2yer]], [[2yex]], [[2ym3]], [[2ym4]], [[2ym5]], [[2ym6]], [[2ym7]], [[2ym8]], [[2ywp]], [[3jvr]], [[3jvs]], [[3nlb]], [[3ot3]], [[3ot8]], [[3pa3]], [[3pa4]], [[3pa5]], [[3tkh]], [[3tki]], [[3u9n]], [[4fsm]], [[4fsn]], [[4fsq]], [[4fsr]], [[4fst]], [[4fsu]], [[4fsw]], [[4fsy]], [[4fsz]], [[4ft0]], [[4ft3]], [[4ft5]], [[4ft7]], [[4ft9]], [[4fta]], [[4ftc]], [[4fti]], [[4ftj]], [[4ftk]], [[4ftl]], [[4ftm]], [[4ftn]], [[4fto]], [[4ftq]], [[4ftr]], [[4ftt]], [[4ftu]], [[4gh2]], [[4hyh]], [[4hyi]], [[4jik]], [[4qye]], [[4qyf]], [[4qyg]], [[4qyh]], [[4rvk]], [[4rvl]], [[4rvm]], [[5dls]], [[5f4n]], [[5fcf]], [[5fck]], [[6fc8]], [[6fcf]], [[6fck]], [[7bko]], [[8e80]], [[8e81]] - hChk1 kinase domain + inhibitor 
**[[5oot]], [[5op2]], [[5op4]], [[5op5]], [[5op7]], [[5opb]], [[5opr]], [[5ops]], [[5opu]], [[5opv]], [[5oq5]], [[5oq6]], [[5oq7]], [[5oq8]], [[7bjd]], [[7bjh]], [[7bjj]], [[7bjm]], [[7bjo]], [[7bjr]], [[7bjx]], [[7bk1]], [[7bk2]], [[7bk3]], [[7mck]], [[7suf]], [[7sug]], [[7suh]], [[7sui]], [[7suj]], [[8siv]], [[8siw]], [[8six]] - hChk1 kinase domain (mutant) + inhibitor
**[[5oop]] - hChk1 kinase domain (mutant) + AMPPNP
**[[5oor]] - hChk1 kinase domain (mutant) + staurosporine
**[[7bkn]] - hChk1 kinase domain + adenine
**[[7bje]] - hChk1 kinase domain (mutant) + adenine
**[[2jqi]] – yChk1 – yeast
*'''Chk2 (Checkpoint kinase)'''
**[[1gxc]] – hChk2 phosphothreonine-binding domain + phosphopeptide
**[[2cn5]] – hChk2 kinase domain + ADP
**[[2cn8]] – hChk2 kinase domain + inhibitor
**[[2cn8]], [[2uv2]], [[2w0j]], [[2w7x]], [[2wtc]], [[2wtd]], [[2wti]], [[2wtj]], [[2xbj]], [[2xk9]], [[2xm8]], [[2xm9]], [[2ycf]], [[2ycq]], [[2ycr]], [[2ycs]], [[2yiq]], [[2yir]], [[2yit]], [[4a9r]], [[4a9s]], [[4a9t]], [[4bda]], [[4bdb]], [[4bdc]], [[4bdd]], [[4bde]], [[4bdf]], [[4bdg]], [[4bdh]], [[4bdi]], [[4bdj]], [[4bdk]] - hChk2 kinase domain + inhibitor
**[[3i6u]], [[3i6w]] – hChk2 residues 84-502 (mutant)
*'''Chk3 (Mst2)'''; domains - kinase 13-313; SARAH 436-484
**[[4hkd]], [[4l0n]], [[4oh9]], [[3wws]] – hChk3 SARAH domain
**[[4lg4]] – hChk3 kinase domain
**[[4lgd]] – hChk3 kinase domain + RASSF5 SARAH domain
**[[6ao5]] – hChk3 kinase+SARAH domains (mutant) + SAV1 SARAH domain
**[[5dh3]], [[8a66]] – hChk3 kinase domain + inhibitor
*'''Chk4 (Mst1)''' ; Domains – kinase 1-311; SARAH 432-480
**[[3com]] – hChk4 kinase domain
**[[6yat]], [[8a5j]]– hChk4 kinase domain + inhibitor
**[[4nr2]] – hChk4 SARAH domain
**[[2jo8]] – hChk4 SARAH domain - NMR
**[[4oh8]] – hChk4 SARAH domain + Ras association domain-containing protein
*'''Chk5 (Aurora kinase b)'''
**[[4af3]] – hChk5 + inhibitor
*'''Chk6 or Chk15 or Aurora kinase A'''
**[[1muo]], [[1mq4]], [[4j8n]], [[6cpe]], [[4o0s]] – hChk6 kinase domain
**[[4bn1]], [[4o0w]], [[4o0u]] – hChk6 kinase domain (mutant)
**[[5dnr]], [[5drd]], [[5dt3]] – hChk6 kinase domain + ATP
**[[5drd]] – hChk6 kinase domain + ATP
**[[1ol6]] – hChk6 kinase domain (mutant) + ATP
**[[2wqe]] – hChk6 kinase domain (mutant) + ADP
**[[5odt]] – hChk6 kinase domain (mutant) + ADP + TACC3
**[[2c6d]] – hChk6 kinase domain (mutant) + ADPNP
**[[2dwb]] – hChk6 kinase domain + AMPPNP
**[[6cpf]] – hChk6 kinase domain + AMPPCP
**[[5g15]] – hChk6 kinase domain + AMPPNP + monobody
**[[6cpg]], [[8ssp]] – hChk6 kinase domain + inhibitor + monobody
**[[2j4z]], [[2j50]], [[2np8]], [[3efw]], [[2x81]], [[2x6d]], [[2x6e]], [[3myg]], [[3vap]], [[4b0g]], [[4j8m]], [[5dpv]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5one]], [[5obr]], [[4byi]], [[4byj]], [[4jai]], [[4jaj]], [[3w10]], [[3w16]], [[3w18]], [[3w2c]], [[4uzh]], [[4uzd]], [[4uyn]], [[4zs0]], [[4ztq]], [[4ztr]], [[4zts]], [[5aad]], [[5aae]], [[5aag]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5obr]], [[5one]], [[6gra]], [[6c2t]], [[6c2r]], [[5zan]], [[6z4y]], [[7ayh]], [[7ayi]], [[7fic]], [[7o2v]], [[8jmx]] – hChk6 kinase domain + inhibitor
**[[2bmc]], [[2c6e]], [[3coh]], [[3h0y]], [[3h0z]], [[3h10]], [[3fdn]], [[2wtw]], [[3lau]], [[3nrm]], [[2xne]], [[2xng]], [[2xru]], [[3k5u]], [[3m11]], [[3p9j]], [[3r21]], [[3r22]], [[3qbn]], [[3unz]], [[3uo4]], [[3uo5]], [[3uo6]], [[3uod]], [[3uoh]], [[3uoj]], [[3uok]], [[3uol]], [[3up2]], [[3up7]], [[4dhf]], [[4dea]], [[4deb]], [[4ded]], [[4dee]], [[5aad]], [[5aae]], [[5aaf]], [[5aag]], [[4jbo]], [[4jbp]], [[4jbq]], [[4prj]], [[5dpv]], [[6hjk]], [[6hjj]] – hChk6 kinase domain (mutant) + inhibitor
**[[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[5dos]], [[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5dn3]], [[5dos]], [[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[6c83]] – hChk6 kinase domain + AMPPCP + nanobody
**[[8sso]] – hChk6 kinase domain + drug + monobody
**[[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5g1x]], [[7ztl]] – hChk6 kinase domain (mutant) + N-Myc
**[[8guw]] – hChk6 kinase domain/activator peptide
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + Targeting protein for XKLP2
**[[3daj]], [[3d14]], [[3dj5]], [[3dj6]], [[3dj7]], [[3d15]], [[3d2i]], [[3d2k]] – Chk6 kinase domain (mutant) + inhibitor - mouse
*Chk6 with phosphorylated Thr 287, Thr288
**[[1ol5]], [[1ol7]] – hChk6 kinase domain + PThr + ADP
**[[5dnr]], [[5dt3]] – hChk6 kinase domain + PThr + ATP
**[[2w1c]], [[2w1d]], [[2w1e]], [[2w1f]], [[2w1g]], [[5dn3]] – hChk6 kinase domain + PThr + inhibitor
**[[2wtv]], [[5orl]], [[5orn]], [[5oro]], [[5orp]], [[5orr]], [[5ors]], [[5ort]], [[5orv]], [[5orw]], [[5orx]], [[5ory]], [[5orz]], [[5os0]], [[5os1]], [[5os2]], [[5os3]], [[5os4]], [[5os5]], [[5os6]], [[5osd]], [[5ose]], [[5osf]] – hChk6 kinase domain (mutant) + PThr + inhibitor
**[[3e5a]], [[3ha6]] – hChk6 kinase domain + PThr + inhibitor + targeting protein for XKLP2
**[[5g1x]] – hChk6 kinase domain (mutant) + PThr + N-Myc
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + PThr + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + PThr + TPX2
**[[6r4d]], [[6r4c]], [[6r4b]], [[6r4a]] – hChk6 kinase domain + PThr + inhibitor + ADP
**[[6i2u]] – hChk6 kinase domain (mutant) + PThr + inhibitor + ADP
**[[6r49]] – hChk6 kinase domain (mutant) + PThr + CoA
*'''Chk10 (lymphocyte-oriented kinase)''' or LOK or STK10
**[[7qgp]] – hChk10
**[[2j7t]], [[4aot]], [[4equ]], [[4usd]], [[4use]], [[5ajq]], [[5owq]], [[5owr]], [[6eim]], [[6gtt]], [[6i2y]], [[6hxf]] – hChk10 kinase domain + inhibitor
**[[4bc6]], [[6i2y]] – hChk10 + drug
*'''Chk11'''
**[[2wtk]] – hChk11 (mutant) + calcium-binding protein
*'''Chk12-A (Aurora kinase b-a or Aurora B kinase)'''
**[[2vgo]], [[2vgp]], [[2vrx]], [[3ztx]], [[4c2v]], [[5eyk]] – fChk12-A + inner centromere protein A peptide + inhibitor - frog
**[[4c2w]] – fChk12-A + inner centromere protein A peptide + AMPPNP
**[[4b8l]], [[4b8m]], [[5k3y]] – fChk12-A (mutant) + inner centromere protein A peptide + inhibitor
*'''Chk13 (Polo-like kinase Plk)'''
*Plk1 Polo-box domain (Pbd) 371-594''
**[[1q4o]], [[2ogq]], [[3hih]], [[3p2w]], [[4h5x]], [[6n46]] – hPlk1 Pbd
*Plk1 Pbd complex with polypeptide
**[[1umw]], [[2ojx]], [[3bzi]], [[3c5l]], [[3rq7]], [[4dfw]], [[4whl]], [[4whk]], [[4whh]], [[4rcp]], [[4o6w]], [[4o56]], [[5dms]], [[5dmv]], [[5dnj]] , [[7mso]], [[7mx1]] – hPlk1 + peptide
**[[3hik]], [[3fvh]], [[3p2z]], [[3p34]], [[3p35]], [[3p36]], [[3p37]], [[3q1i]], [[4e67]], [[4e9c]], [[4e9d]], [[4hab]], [[4hy2]], [[4o9w]], [[4x9r]], [[4x9v]], [[4x9w]], [[5j19]], [[6gy2]] – hPlk1 + phosphopeptide
**[[1q4k]] – hPlk1 (mutant) + phosphopeptide
**[[2v5q]] – hPlk1 + design ankyrin repeat protein
**[[4lkl]] – hChk Plk1 + PL-55
**[[4lkm]] – hChk Plk1 + PL-74
**[[6ax4]] – hChk Plk1 + histidine cyclized macrocycle
**[[5x3s]] – mPlk1 + phosphopeptide
**[[8joq]], [[8joy]] – hPlk1 Pbd + hpv peptide
*Plk1 Pbd complex with small molecule inhibitor
**[[4h71]], [[4hco]], [[5ta6]], [[5ta8]], [[8bjt]], [[8crc]] – hPlk1 + inhibitor
**[[2rku]] – hPlk1 (mutant) + inhibitor
**[[3db6]], [[3db8]], [[3dbc]], [[3dbd]], [[3dbe]], [[3dbf]] – zfPlk1 (mutant) + inhibitor – zebra fish
*Plk1 catalytic domain 36-345
**[[2owb]] – hPlk1 catalytic domain (mutant)
**[[2ou7]] – hPlk1 catalytic domain (mutant) + AM
**[[3kb7]], [[2yac]], [[3thb]], [[4a4l]], [[4a4o]] – hPlk1 catalytic domain + inhibitor
**[[3fc2]] – hPlk1 catalytic domain (mutant) + inhibitor
**[[4j52]], [[4j53]] – hChk Plk1 (mutant) + inhibitor
**[[3d5x]] – zfPlk1 catalytic domain (mutant) + wortmannin
**[[3d5w]] – zfPlk1 catalytic domain + ADP
*'''Plk2'''
**[[4i5m]], [[4i5p]], [[4i6b]], [[4i6f]], [[4i6h]] – hChk Plk2 kinase domain (mutant) + inhibitor
**[[4xb0]], [[4rs6]] – hChk Plk2 Pbd
*'''Plk3'''
**[[4b6l]], [[4i6b]] – hChk Plk3 kinase domain + inhibitor
*'''Plk4'''; Domains – kinase 2-275; Pbd 580-808; Pb3 884-970
**[[3cok]] – hChk Plk4 kinase domain
**[[4n9j]] – hChk Plk4 Pbd domain
**[[4n7z]], [[4n7v]] – hChk Plk4 Pbd domain + centrosomal protein
**[[6w38]], [[6w3i]] – hChk Plk4 Pbd domain + Fam46C
**[[6w3j]] – hChk Plk4 Pbd domain + Fam46C + CEP92 peptide
**[[4jxf]], [[4yur]] – hChk Plk4 kinase domain + inhibitor
**[[5lhy]] – hChk Plk4 Pb3 domain
**[[4yyp]], [[5lhz]] – hChk Plk4 Pb3 domain + Scl-interrupting locus protein
**[[4nk7]], [[4g7n]], [[5lhx]], [[7rl3]] – DmChk Plk4 Pbd domain – ''Drosophila melanogaster''
*'''Chk16'''
**[[2buj]] – hChk16 (mutant) + staurosporin
*'''Chk17B''' or DRAK2 or STK17B
**[[3lm0]] – hChk17B
**[[6qf4]], [[7q7c]], [[7q7d]] – hChk17B + ADP
**[[7q7e]] – hChk17B + ATP
**[[3lm5]] – hChk17B + quercetin
**[[6y6f]], [[6y6h]], [[6zjf]] – hChk17B + pyrimidine derivative
**[[7akg]] – hChk17B + drug
*'''Chk19''' or STK19
**[[7xrb]] – hChk19
*'''Chk24 (Mst3)''' or STK24
**[[3a7f]], [[3a7g]], [[3a7h]], [[3a7i]], [[3a7j]], [[3ckw]] – hChk24 kinase domain
**[[4w8e]], [[4w8d]], [[4u8z]], [[4qmm]], [[4qmn]], [[4qmo]], [[4qmp]], [[4qmq]], [[4qms]], [[4qmt]], [[4qmu]], [[4qmv]], [[4qmw]], [[4qmx]], [[4qmy]], [[4qmz]], [[4qna]], [[4qo9]], [[4u8z]], [[7b30]], [[7b31]], [[7b32]], [[7b33]], [[7b34]], [[7b35]], [[8bzi]], [[8bzj]], [[8qlr]], [[8qls]], [[8qlt]] – hChk Mst3 + inhibitor
**[[8qlq]] – hChk Mst3 + macrocyclic inhibitor
**[[3ckx]] – hChk24 kinase domain + staurosporin
**[[3zhp]] – hChk24 kinase domain + calcium-binding protein
**[[4o27]] – hChk24 kinase domain (mutant) + calcium-binding protein
**[[4qml]] – hChk Mst3 kinase domain + AMPPNP
*'''Chk25 or STK25'''
**[[2xik]] – hChk25 kinase domain
**[[7z4v]] – hChk25 kinase domain + inhibitor
**[[3w8h]] – hChk25 regulatory domain + programmed cell death protein 10
**[[4nzw]] – hChk25 kinase domain (mutant) + calcium-binding protein
*'''Chk26 (Mst4)'''
**[[3ggf]], [[7b36]] – hChk Mst4 + inhibitor
**[[4geh]], [[3w8i]] - hChk Mst4 dimerization domain + programmed cell death protein 10
**[[4fza]], [[4fzd]], [[4fzf]] – hChk Mst4 (mutant) + calcium-binding protein
*'''Chk32'''
**[[4fr4]] – hChk32A
*'''Chk38'''
**[[6bxi]] – hChk38 kinase domain
*'''Chk39''' or SPAK
**[[7o86]] – hChk39 C-terminal
**[[5d9h]] – mChk39 residues 63-403 + ATP
**[[5dbx]] – mChk39 residues 63-403 (mutant) + AMPPNP
*'''Chk40'''
**[[5l2q]] – hChk40 kinase homology domain
*'''Dclk1'''
**[[6kyq]] – hChk Dclk1 kinase domain
**[[6kyr]] – hChk Dclk1 kinase domain (mutant)
**[[5jzj]] – hChk Dclk1 kinase domain + AMPPN
**[[5jzn]], [[7kx6]], [[7kxw]] – hChk Dclk1 kinase domain + inhibitor
**[[7f3g]] – hChk Dclk1 kinase domain + drug
**[[7kx8]] – hChk Dclk1 C-terminal + inhibitor
*'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123; kinase 144-480
**[[1unp]], [[1unr]] – hRac-α hChk pleckstrin homology domain
**[[2uzr]], [[2uzs]], [[7myx]] – hRac-α hChk pleckstrin homology domain (mutant)
**[[1h10]], [[1unq]], [[2uvm]] – hRac-α hChk pleckstrin homology domain + inositol tetrakisphosphate
**[[3o96]], [[4ejn]], [[6s9w]], [[6s9x]], [[6hhj]], [[6hhi]], [[6hhh]], [[6hhg]], [[6hhf]] - hRac-α hChk + inhibitor
**[[5kcv]], [[7nh4]], [[7nh5]] - hRac-α hChk (mutant) + inhibitor
**[[4gv1]], [[4ekl]] - hRac-α hChk kinase domain + inhibitor
**[[3qkm]], [[6ccy]] - hRac-α hChk kinase domain (mutant) + inhibitor
**[[6buu]] - hRac-α hChk kinase domain + bisubstrate peptide
**[[4ekk]] - hRac-α hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[6npz]] - hRac-α hChk kinase domain + peptide + inhibitor
**[[3ow4]], [[3qkk]], [[3qkl]], [[6buu]] - hRac-α hChk kinase domain (mutant) + peptide + inhibitor
**[[7apj]] - hRac-α hChk + nanobody
*'''Rac-β hChk (AKT2)'''
**[[1gzk]], [[1gzn]], [[1gzo]], [[1mrv]], [[1mry]] – hRac-β hChk kinase domain
**[[1p6s]] - hRac-β hChk pleckstrin homology domain - NMR
**[[1o6k]] - hRac-β hChk kinase domain + GSK3 peptide + AMPPNP
**[[2jdo]], [[2jdr]], [[2uw9]], [[2x39]], [[3cqu]], [[3cqw]] - hRac-β hChk kinase domain + GSK3 peptide + inhibitor
**[[3e87]], [[3e88]], [[3e8d]] - Rac-β hChk kinase domain (mutant) + GSK3 peptide + inhibitor<br /
**[[1o6l]] - hRac-β hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[3d0e]], [[8q61]] - hRac-β hChk kinase domain (mutant) + inhibitor
*'''Rac-γ hChk (ATK3)'''
**[[2x18]] – Rac-γ hChk PH domain
*'''A-Raf'''
**[[1wxm]] – hA-Raf RAS-binding domain 19-91 - NMR
**[[2mse]] – hA-Raf RAS-binding domain + APOA-I + K-ras - NMR
*'''B-Raf'''; domains - BRS 38-116; Ras-binding 153-237; kinase 445-723
**[[8dgs]], [[8dgt]] – hB-Raf in Ras/Raf complex – Cryo EM
**[[7z37]], [[7z38]], [[7zr5]] – hB-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
**[[1uwh]], [[3c4c]], [[6v2u]], [[6xfp]], [[6xlo]], [[8f7o]], [[8f7p]] – hB-Raf kinase domain + anticancer drug
**[[1uwj]], [[6p3d]] – hB-Raf kinase domain (mutant) + anticancer drug
**[[2fb8]], [[3d4q]], [[3ii5]], [[3psd]], [[3skc]], [[3tv6]], [[4g9c]], [[4ksp]], [[4ksq]], [[3psb]], [[3ppj]], [[3ppk]], [[3prf]], [[3pri]], [[3tv4]], [[4dbn]], [[4e4x]], [[4mbj]], [[4ehe]], [[3q4c]], [[3q96]], [[3e26]], [[4h58]], [[4e26]], [[4fc0]], [[4pp7]], [[6cad]], [[7shv]] – hB-Raf kinase domain + pyrazole inhibitor
**[[4jvg]], [[4ehg]], [[4fk3]], [[3idp]], [[4g9r]], [[4wo5]], [[4mnf]], [[4r5y]], [[4rzv]], [[4rzw]], [[4xv1]], [[4xv2]], [[4xv3]], [[4xv9]], [[4yht]], [[5c9c]], [[5hi2]], [[5ita]], [[5jrq]], [[5jsm]], [[5jt2]], [[6nsq]], [[6p7d]], [[6uuo]] – hB-Raf kinase domain (mutant) + pyrazole inhibitor
**[[5csw]], [[5csx]], [[5ct7]], [[5fd2]], [[5hid]], [[5hie]], [[5val]], [[5vam]], [[6b8u]], [[6n0q]], [[6n0p]], [[7k0v]], [[7p3b]], [[7p3v]], [[8c7x]], [[8c7y]] - hB-Raf kinase domain + inhibitor
**[[6v34]] – hB-Raf kinase domain (mutant) + inhibitor
**[[4mne]] – hB-Raf kinase domain + MAPKK1
**[[8f7o]] – hB-Raf kinase domain + drug
**[[7m0u]] – hB-Raf kinase domain + AMPPNP + drug
**[[6u2h]] – hB-Raf kinase domain + 14-3-3 ζ/δ
**[[7mfe]] – hB-Raf + 14-3-3 ζ/δ – Cryo EM
**[[7mff]] – hB-Raf + 14-3-3 ζ/δ + inhibitor – Cryo EM
**[[7mfd]] – hB-Raf + 14-3-3 ζ/δ + MEK + inhibitor – Cryo EM
**[[6pp9]] – hB-Raf kinase domain + MEK1 + ANP
**[[7m0x]], [[7m0z]] – hB-Raf kinase domain + MEK1 + ANP + inhibitor
**[[7m0t]], [[7m0u]], [[7m0v]], [[7m0w]], [[7m0y]] – hB-Raf kinase domain + MEK1 + ANP + drug
**[[6u2g]] – hB-Raf kinase domain + MEK1 + AMPPCP
**[[5vr3]] – hB-Raf BRS domain
**[[7jhp]] – hB-Raf BRS domain + Hras
**[[6ntc]], [[6ntd]] – hB-Raf BRS domain (mutant) + Hras
**[[6xi7]] – hB-Raf 52-188 + Kras
**[[2l05]], [[5j17]], [[5j2r]] – hB-Raf RAS-binding domain - NMR
**[[3ny5]] – hB-Raf RAS-binding domain
**[[5j18]] – hB-Raf RAS-binding domain + inhibitor - NMR
**[[6pts]], [[6ptw]] – hB-Raf 56-187 + Kras + apolipoprotein + GMPPNP - NMR
**[[6uan]], [[6q0k]] – hB-Raf + 14-3-3 ζ – Cryo EM
**[[6nyb]] – hB-Raf + 14-3-3 ζ + MEK1 – Cryo EM
**[[6q0t]], [[6q0j]] – hB-Raf (mutant) + 14-3-3 ζ + MEK1 – Cryo EM
*'''c-Raf'''; Domains – RAS-binding (RBD) 55-132; Cys-rich 136-187 (CBD); kinase 323-618
**[[1rfa]], [[8jna]], [[8jof]], [[8jog]] – hc-Raf RBD - NMR
**[[1faq]], [[1far]] – hc-Raf cysteine-rich domain - NMR
**[[3omv]] – hc-Raf kinase domain
**[[1rrb]] – c-Raf RBD – NMR - rat
*c-Raf complex with protein
**[[8cpd]] – hc-Raf + 14-3-3 protein zeta – Cryo EM
**[[9mmp]] – hc-Raf + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[9mmr]] – hc-Raf (mutant) + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[1c1y]] – hc-Raf RBD + RAP1A
**[[3kuc]] – hc-Raf RBD (mutant) + RAP1A
**[[1gua]] – hc-Raf RBD + RAP1A + GPPNHP
**[[8jnb]] – hc-Raf RBD + ligand
**[[4g0n]], [[4g3x]] – hc-Raf RBD + GTPase Hras
**[[3kud]] – hc-Raf RBD (mutant) + GTPase Hras
**[[8epw]], [[8t74]] – hc-Raf RBD + GTPase K-ras
**[[8t75]], [[9ygs]] – hc-Raf RBD-CRD + GTPase K-ras + GMPPNP
**[[9ay7]], [[9aya]] – hc-Raf + MEK1
**[[9mmq]] – hc-Raf + MEK1 – Cryo EM
**[[9mms]] – hc-Raf (mutant) + MEK1 – Cryo EM
**[[9o0u]], [[9o0v]] – hc-Raf (mutant) + MEK1 + ANP + inhibitor– Cryo EM
**[[8u1l]] – hc-Raf + Hsp90 + CDC37 – Cryo EM
**[[8gae]], [[8gft]] – hc-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
*'''Snf1-related Chk'''
**[[3uc4]], [[3uc3]], [[3udb]], [[3zut]], [[3zuu]] – AtChk Srk2E kinase domain (mutant) – ''Arabidopsis thaliana''
**[[3ujg]] – AtChk Srk2E kinase domain (mutant) + protein phosphatase 2C
**[[5yks]] – hChk
*'''MAPK-interacting Chk''' or Mnk1 Mnk2
**[[2hw6]] – hMnk 1 catalytic domain
**[[2hw7]] – hMnk 1 catalytic domain + staurosporin
**[[5wvd]] – hMnk 1 catalytic domain + inhibitor
**[[2ac3]] – hMnk 2 catalytic domain
**[[2ac5]] – hMnk 2 catalytic domain (mutant)
**[[6cj5]], [[6cje]], [[6cjh]], [[6cjw]], [[6cjy]], [[6ck3]], [[6ck6]], [[6cki]] – hMnk 2 catalytic domain (mutant) + inhibitor
*'''hChk Pak''' or '''Chk N''' or '''PRK1'''; Domains - CRIB 74-109; Hr1B 122-199; catalytic 109-426; kinase 605-942
**[[1urf]] – hChk Pak-1 Hr1b domain - NMR
**[[4nkg]] – hChk Pak-1 Hr1b domain + SSPH1 LRR domain
**[[2rmk]] – hChk Pak-1 Hr1bb domain + Rac1 - NMR
**[[1f3m]] – hChk Pak-1 autoregulatory+kinase domains
**[[4otd]] - hChk Pak-1 kinase domain
**[[1yhv]], [[1yhw]], [[3q4z]], [[3q52]], [[3q53]] – hChk Pak-1 kinase domain (mutant)
**[[4o0r]], [[4o0t]], [[4zji]], [[4zjj]], [[4zlo]], [[4zy4]], [[4zy5]], [[4zy7]], [[5ime]], [[5kbq]], [[5kbr]], [[6b16]], [[7vto]] – hChk Pak-1 kinase domain + inhibitor
**[[4oti]], [[4oth]], [[4otg]] – hChk Pak-1 kinase domain + inhibitor
**[[4eqc]], [[4p90]], [[5dew]], [[5dey]], [[5dfp]] – hChk Pak-1 kinase domain (mutant) + inhibitor
**[[2hy8]] – hChk Pak-1 kinase domain + staurosporin
**[[2qme]] – hChk Pak-1 CRIB domain + RAC3
**[[3fxz]], [[3fy0]], [[4daw]] – hChk Pak-1 kinase domain (mutant) + Ru complex
**[[6fd3]] – hChk Pak-3 kinase domain (mutant)
**[[2j0i]], [[4fie]] – hChk Pak-4
**[[4fig]], [[4fij]], [[4l67]] – hChk Pak-4 kinase domain
**[[2cdz]] – hChk Pak-4 + purine derivative
**[[2ov2]] – hChk Pak-4 CRIB domain + RAC3
**[[2qon]], [[4fif]], [[4fih]], [[4fii]], [[4jdh]], [[4jdi]], [[4jdj]], [[4jdk]], [[6wlx]], [[6wly]] – hChk Pak-4 kinase domain + peptide
**[[4app]], [[4o0v]], [[4o0x]], [[4o0y]], [[4njd]], [[4xbu]], [[5bms]], [[5i0b]], [[5vee]], [[5vef]], [[5zjw]], [[5xvg]], [[5xvf]], [[5xva]], [[7cmb]], [[7cp3]], [[7cp4]] – hChk Pak-4 kinase domain + inhibitor
**[[2x4z]], [[2xh5]] – hChk Pak-4 kinase domain (mutant) + inhibitor
**[[5upl]], [[5upk]] – hChk Pak-4 kinase domain (mutant) + CDC42
**[[5ved]] – hChk Pak-4 kinase domain + staurosporine
**[[8ahi]] – hChk Pak-4 300-591 + inhibitor
**[[7s46]], [[7s48]] – hChk Pak-4 catalytic domain + integrin beta-5 peptide
**[[2c30]] – hChk Pak-6
**[[2odb]] – hChk Pak-6 CRIB domain + CDC42
**[[4ks8]] – hChk Pak-6 kinase domain + sunitinib
**[[4ks7]] – hChk Pak-6 kinase domain (mutant) + inhibitor
**[[2f57]] – hChk Pak-7
*'''Mycobacterium tuberculosis Chk Pkn'''
**[[4x3f]] - MtChk PknA – ''Mycobacterium tuberculosis''
**[[4ow8]] - MtChk PknA kinase domain
**[[3ori]], [[3ork]], [[3orl]], [[3orm]], [[3oro]], [[3orp]], [[3ort]] - MtChk PknB kinase domain (mutant)
**[[1o6y]] – MtChk PknB kinase domain
**[[6b2p]], [[6b2q]] – MtChk PknB kinase domain + inhibitor
**[[2kud]], [[2kue]], [[2kuf]], [[2kui]] – MtChk PknB pasta domains 2-3 - NMR
**[[3ouv]] – MtChk PknB pasta domain 3
**[[5e0y]] – MtChk PknB pasta domain 4
**[[5e10]] – MtChk PknB pasta domains 1-2
**[[5e0z]] – MtChk PknB pasta domains 3-4
**[[5e12]] – MtChk PknB pasta domains 2-4
**[[5u94]] - MtChk PknB kinase domain + inhibitor
**[[3f61]], [[3f69]] - MtChk PknB kinase domain (mutant) + inhibitor
**[[6i2p]] - MtChk PknB kinase domain (mutant) + GARA + peptide
**[[1rwi]], [[1rwl]] - MtChk PknD extracellular domain
**[[2h34]] – MtChk PknE catalytic domain
**[[7naa]] – MtChk PknF kinase domain + inhibitor
**[[4y12]] - MtChk PknG + ATP-gS
**[[4y0x]] - MtChk PknG + ADP
**[[7q52]] - MtChk PknG + inhibitor
**[[4esq]] - MtChk PknH extracellular domain
**[[5m06]], [[5xka]] - MtChk PknI kinase domain
**[[5m07]], [[5m08]], [[5m09]] - MtChk PknI kinase domain (mutant)
**[[5xlm]], [[5xll]] - MtChk PknI sensor domain
**[[7mxb]], [[7mxj]], [[7mxk]] - Chk PknG kinase domain + AMPPNP - Corynebacterium glutamicum
*'''hChk Nek'''
**[[4apc]] – hChk Nek1 kinase domain (mutant)
**[[4b9d]] - hChk Nek1 kinase domain (mutant) + inhibitor
**[[2w5h]] – hChk Nek2 kinase domain
**[[2jav]], [[2wqo]], [[2xk3]], [[2xk4]], [[2xk6]], [[2xk7]], [[2xk8]], [[2xkc]], [[2xkd]], [[2xke]], [[2xkf]], [[2xnm]], [[2xnn]], [[2xno]], [[2xnp]], [[4a4x]], [[4afe]], [[5m51]], [[5m53]], [[5m55]], [[5m57]], [[6sgd]], [[6sgh]], [[6sgi]], [[6sgk]], [[6sk9]] – hChk Nek2 + inhibitor
**[[2w5a]], [[2w5b]] – hChk Nek2 + nucleotide
**[[6tm5]] - hChk Nek2 in anaphase-promoting complex – Cryo EM
**[[2wqm]], [[6s76]] – hChk Nek7
**[[2wqn]] – hChk Nek7 + ADP
**[[5de2]] – hChk Nek7 + hChk Nek9
**[[6s73]], [[2wqo]] – hChk Nek7 + inhibitor
**[[6npy]] – hChk Nek7 + Nlrp3
**[[6s75]] – hChk Nek7 + inhibitor
*'''Chk Rio'''
**[[6fdo]], [[6fdn]], [[6fdm]] – hChk Rio2
**[[4otp]] – hChk Rio1 Rio domain + ADP
**[[6hk6]], [[7vbt]] – hChk Rio2 + inhibitor
**[[6eml]], [[6fai]], [[6g18]], [[6g51]], [[6rbd]],[[6rbe]], [[6y7c]] – yChk Rio2 in 40S particle – Cryo EM
**[[1ztf]] – AfChk Rio1 + adenine derivative – Archaeoglobus fulgidus
**[[1zth]] – AfChk Rio1 + ADP
**[[1zp9]] – AfChk Rio1 + ATP
**[[1tqp]], [[1zao]] – AfChk Rio2 + ATP
**[[1zar]] – AfChk Rio2 + ADP
**[[4gyg]] – CtChk Rio2 – Chaetonium thermophilum
**[[4gyi]] – CtChk Rio2 + ADP
*hChk Vrk (vaccinia-related kinase)
**[[2kty]], [[2kul]], [[2lav]], [[2rsv]] – hChk Vrk1 kinase domain 1-396 - NMR
**[[3op5]] – hChk Vrk1 kinase domain (mutant)
**[[5ukf]] – hChk Vrk1 kinase domain + inhibitor
**[[5uvf]], [[6cnx]], [[6bu6]], [[6cfm]], [[6dd4]], [[6bp0]], [[6bru]], [[6btw]], [[6cmm]], [[6cqh]], [[6csw]], [[6npn]], [[6vxu]], [[6vzh]] – hChk Vrk1 kinase domain (mutant) + inhibitor
**[[6ac9]] – hChk Vrk1 kinase domain (mutant) + AMPPNP
**[[7tan]] – hChk Vrk1 kinase domain + nucleosome – Cryo EM
**[[2v62]] – hChk Vrk2 kinase domain
**[[5uu1]], [[6ncg]], [[8q1z]] – hChk Vrk2 kinase domain + inhibitor
*Chk Wnk (protein kinase lysine-deficient); Domains - kinase 194-483; CCT1 454-549
**[[6cn9]], [[4q2a]], [[4pwn]] - hChk Wnk1 kinase domain (mutant)
**[[5tf9]] - hChk Wnk1 kinase domain + inhibitor + AMPPNP
**[[5wdy]], [[5we8]] - hChk Wnk1 kinase domain + inhibitor + ANP
**[[5drb]], [[6ol2]]- rChk Wnk1 kinase domain (mutant) + inhibitor
**[[6elm]] - hChk Wnk2 CCT1 domain
**[[6fbk]] - hChk Wnk2 CCT1 domain + Wnk1 peptide
**[[5o1v]], [[5o21]], [[5o23]] - hChk Wnk3 kinase domain
**[[5o2c]] - hChk Wnk3 kinase + CCT1 domains
**[[5o26]], [[5tf9]] - hChk Wnk3 kinase domain + AMPPNP
**[[5o2b]] - hChk Wnk3 kinase domain + inhibitor
**[[8edh]] - hChk Wnk3 kinase domain (mutant) + inhibitor
**[[2lru]] – rChk Wnk1 autoinhibitory domain 480-572 - NMR
**[[5w7t]] - rChk Wnk1 kinase domain
**[[7uos]] - rChk Wnk1 kinase domain (mutant)
*'''TANK-binding kinase'''
**[[4efo]] – hChk Tbk1 ubiquitin-like domain
**[[6rsr]], [[6rsu]] – hChk Tbk1 + inhibitor
**[[4im0]], [[4im2]], [[4im3]], [[4iw0]], [[4iwo]], [[4iwp]], [[4ipq]], [[6rst]] – hChk Tbk1 (mutant) + inhibitor
**[[6cq5]], [[6cq4]], [[6cq0]], [[6boe]], [[6bod]], [[6bny]], [[5w5v]] – hChk Tbk1 + ulcer drug
**[[4eut]], [[4euu]] – hChk Tbk1 kinase+ubiquitin-like domains (mutant) + inhibitor
**[[6nt9]] – hChk Tbk1 (mutant) + STING
**[[5eoa]], [[5eof]] – hChk Tbk1 residues 677-729 + optineurin
**[[4jl9]], [[4jlc]] – mChk Tbk1 + inhibitor
**[[6o8c]], [[6o8b]] – mChk Tbk1 (mutant) + STING
*'''Haspin'''
**[[2vuw]], [[2wb8]] – hChk Haspin kinase domain
**[[3dle]] – hChk Haspin kinase domain + AMP
**[[3e7v]], [[3f2n]], [[3fmd]], [[3iq7]], [[4qtc]], [[5htb]], [[5htc]], [[6z56]], [[6z57]], [[6z58]], [[6z59]], [[6z5a]], [[6z5b]], [[6z5c]]. [[6z5d]], [[6z5e]] , [[7avq]], [[7ops]] – hChk Haspin kinase domain + inhibitor
**[[7sqm]] – hChk Haspin kinase domain + antimalarial
**[[6g38]], [[6g34]], [[6g35]], [[6g36]], [[6g37]] – hChk Haspin kinase domain + tubercidin derivative
**[[6g39]], [[6g3a]] – hChk Haspin kinase domain (mutant) + tubercidin derivative
**[[4ouc]] – hChk Haspin kinase domain + histone H3 peptide
*'''MAP/microtubule affinity-regulating kinase (MARK)'''
**[[2hak]] – hChk MARK1 catalytic+UBA domains
**[[3ose]] - hChk MARK1 KA1 domain
**[[6c9d]] – hChk MARK1 catalytic+UBA+KA1 domains (mutant)
**[[5eak]], [[5kz7]], [[5kz8]] – hChk MARK2 catalytic+UBA domains + inhibitor
**[[3iec]] – hChk MARK2 catalytic+UBA domains + cytotoxicity-associated immunodominant antigen peptide
**[[2qnj]] – hChk MARK3 catalytic+UBA domains
**[[3fe3]] – hChk MARK3 catalytic+UBA domains (mutant)
**[[7p1l]] – hChk MARK3 catalytic+UBA domains + inhibitor
**[[5es1]] – hChk MARK4 catalytic+UBA domains + inhibitor
**[[1zmu]] – rChk MARK2 catalytic+UBA domains
**[[2wzj]], [[2r0i]], [[1zmv]], [[1y8g]], [[1zmw]] – rChk MARK2 catalytic+UBA domains (mutant)
**[[1ul7]], [[1v5s]] - mChk MARK3 catalytic domain - NMR
*'''Mitotic checkpoint Chk (Bub)'''; Domains: TPR 1-220; kinase 726-1085
**[[2lah]] – hChk Bub1 TPR domain – NMR
**[[2wvi]] – hChk Bub1β TPR domain
**[[3si5]] – hChk Bub1 TPR domain + CASC5 peptide
**[[4r8q]], [[4qpm]], [[5dmz]] – hChk Bub1 kinase domain + ADP
**[[6f7b]] – hChk Bub1 kinase domain + inhibitor
**[[4a1g]] – hChk Bub1 TPR domain + CASC5 KI motif
**[[4ggd]] - hChk Bub1 + cell division cycle protein
**[[6tlj]], [[5khu]] - hChk Bub1 in anaphase-promoting complex – Cryo EM
**[[6jkk]] – DmChk Bub1 kinase domain
**[[6jkm]] – DmChk Bub1 kinase domain + ADP
**[[5jja]] – hChk Bub1 residues 661-734 + PP2A
**[[3esl]] – yChk Bub1 N terminal
**[[4bl0]] - yChk Bub1 + cell cycle arrest protein Bub3
*'''Microtubule-associated Chk'''
**[[2m9x]] – hChk 1 residues 187-287 – NMR
**[[3ps4]] - hChk 1 residues 965-1057
**[[2kqf]], [[2kyl]] – hChk 2 PDZ domain + glycoprotein C terminal – NMR
**[[3khf]] - hChk 3 PDZ domain
**[[2w7r]] – hChk 4 PDZ domain
*'''mTOR''' or '''Mechanistic target of rapamycin'''
*''mTOR FRB domain residues 2015-2114''
**[[1nsg]], [[1fap]] – hFRAP FRB domain + FKBP
**[[2rse]] – hFRAP FRB domain + FKBP – NMR
**[[1aue]] – hFRAP FRB domain
**[[2gaq]], [[2npu]] – hFRAP FRB domain - NMR
**[[8ppz]] – hFRAP FRB domain + FKBP + pyridine derivative
**[[3fap]], [[2fap]], [[4fap]] – hFRAP FRB domain + FKBP + rapamycin analog
**[[4drh]], [[4dri]], [[4drj]], [[5gpg]] – hFRAP FRB domain + FKBP + rapamycin
**[[6m4u]], [[6m4w]] – hChk Mtor FRB domain (mutant) + FKBP1A + rapamycin
**[[5wbh]] – hFRAP FRB domain + S6K1 peptide
*''mTOR FAT+PIKK domain residues 1376-2549''
**[[4jsn]] – hFRAP + TORC subunit LST8
**[[4jsp]] – hFRAP + TORC subunit LST8 + ATP
**[[4jsv]] – hFRAP + TORC subunit LST8 + ADP
**[[4jsx]] – hFRAP + TORC subunit LST8 + torin2
**[[4jt5]] – hFRAP + TORC subunit LST8 + pp242
**[[4jt6]] – hFRAP + TORC subunit LST8 + PI-103
**[[5wby]], [[5wbu]] – hFRAP + TORC subunit LST8 + proline-rich Akt1 substrate
*''mTOR complex''
**[[5flc]] – hmTOR + RAPTOR + LST8 + FKBP – Cryo EM
**[[5h64]] – hmTOR + RAPTOR + LST8 – Cryo EM
**[[6sb2]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC – Cryo EM
**[[6sb0]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC + proline-rich Akt1 substrate – Cryo EM
**[[5zcs]] – hmTOR + LST8 + AVO3 + TORC2 – Cryo EM
**[[7tzo]] – hTORC2 in mTORC2 complex– Cryo EM
**[[6zwm]], [[6zwo]], [[7owg]], [[7pe7]], [[7pe8]], [[7pe9]], [[7pea]], [[7peb]], [[7pec]], [[7uxc]] , [[8era]]– mTOR in mTor complex – Cryo EM
*'''Gcn2'''
**[[1zyc]] – yChk Gcn2
**[[1zxe]], [[1zy4]], [[1zy5]] – yChk Gcn2 (mutant)
**[[2yz0]] – yChk Gcn2 RWD/GI domain – NMR
**[[4otm]] – yChk Gcn2 C terminal domain
**[[1zyd]] – yChk Gcn2 + ATP
**[[4otn]] – mChk Gcn2 C terminal domain
*'''LRRK1''' or leucine-rich repeat Chk1
**[[8e04]], [[8e05]], [[8e06]], [[8fac]] – hLRRK1 – Cryo EM
*'''LRRK2''' or leucine-rich repeat Chk2 or dardarin
**[[6xr4]] – hLRRK2 – Cryo EM
**[[7lht]], [[7lhw]], [[7li4]] – hLRRK2 + ATP + GDP – Cryo EM
**[[7li3]] – hLRRK2 (mutant) + ATP + GDP – Cryo EM
**[[6oje]], [[7thy]] – hLRRK2 GTPase domain 1329-1520
**[[6ojf]] – hLRRK2 GTPase domain (mutant)
**[[6dlo]], [[6dlp]] – hLRRK2 WD40 domain
**[[7thz]] – hLRRK2 1330-1527 + GDP
**[[6vno]], [[6vp6]], [[6vp7]] – hLRRK2 C terminal 1330-2527 – Cryo EM
**[[6vp8]] – hLRRK2 C terminal 1330-2527 + COR domain 1670-1950 + WD40 domain 2140-2489 – Cryo EM
**[[6s6q]] – AtLRRK2 ectodomain + protein casparian strip peptide
*'''Pim'''
*Pim1 catalytic domain residues 14-313
**[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain
**[[1yxs]] – hPim1 catalytic domain (mutant)
**[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP
**[[1yxu]] – hPim1 catalytic domain + AMP
**[[1yxv]], [[5ipj]] – hPim1 catalytic domain + quinoline derivative
**[[1yxx]] – hPim1 catalytic domain + indole derivative
**[[2bzh]], [[2bzi]], [[2bzj]] – hPim1 catalytic domain (mutant) + organometallic ligand
**[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3c4e]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umw]], [[3umx]], [[4enx]], [[4eny]], [[4k1b]], [[4k18]], [[4k0y]], [[4iaa]], [[4i41]], [[4ll5]], [[4lm5]], [[4lmu]], [[4mta]], [[4med]], [[4mbl]], [[4mbi]], [[4n6y]], [[4n6z]], [[4n70]], [[4xh6]], [[5iis]], [[5kgd]], [[5kge]], [[5kgg]], [[5kgi]], [[5kgk]], [[5kzi]], [[5vua]], [[5vub]], [[5vuc]], [[6mt0]], [[6vrv]], [[7oov]], [[7oow]], [[7oox]], [[7xsv]] – hPim1 catalytic domain + inhibitor
**[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor
*Pim1 kinase domain residues 92-404
**[[4jx3]] – hPim1 kinase domain
**[[3uix]], [[5c1q]] – hPim1 kinase domain residues 120-404 + quinoline derivative
**[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate
**[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand
**[[1xws]], [[4alu]], [[4alv]], [[4alw]], [[4as0]], [[4bzn]], [[4bzo]], [[4dtk]], [[4jx7]], [[4rbl]], [[4rc2]], [[4rc3]], [[4rc4]], [[4ty1]], [[4wrs]], [[4wsy]], [[4wt6]], [[4xhk]], [[5dgz]], [[5dhj]], [[5dia]], [[5dwr]], [[5eol]], [[5kcx]], [[5o11]], [[5o12]], [[5o13]], [[5tel]], [[5tex]], [[5toe]], [[5v80]], [[5v82]]. [[6bsk]], [[6kzi]], [[6l11]], [[6l12]], [[6l13]], [[6l14]], [[6l15]], [[6l16]], [[6l17]], [[6no8]], [[6no9]], [[6vru]], [[6ykd]], [[7zun]] – hPim1 kinase domain + inhibitor
**[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor
*Pim1 full length
**[[4rpv]], [[5tur]] - hPim1 + inhibitor
*Pim1 complex with consensus peptide (pimtide)
**[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6qxk]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]] – hPim1 kinase domain + inhibitor + consensus peptide
**[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide
**[[2c3i]], [[5ndt]], [[5n5m]], [[5n5l]], [[5n52]], [[5n51]], [[5n50]], [[5n4z]], [[5n4y]], [[5n4x]], [[5n4v]], [[5n4u]], [[5n4r]], [[5n4o]], [[5n4n]], [[5mzl]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide
**[[4gw8]], [[7qb2]], [[7qfm]], [[7z6u]], [[8afr]] – hPim1 catalytic domain (mutant) + inhibitor + pimtide
**[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide
**[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide
*Pim1 containing phosphorylated Ser 261
**[[1yhs]] – hPim1 kinase domain + PSer + staurosporine
**[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor
**[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor
**[[1yi4]] – hPim1 kinase domain + PSer + adenosine
*Pim2
**[[4x7q]] – hPim2 catalytic domain + inhibitor
**[[2iwi]] – hPim2 catalytic domain + Ru ligand
*'''Rip or receptor-interacting Chk; Domains – catalytic 1-294; Amyloid fibril 418-518; Death 561-671'''
**[[6ac5]] – hRip1 death domain
**[[6r5f]], [[6nw2]], [[6c4d]], [[6c3e]], [[5tx5]], [[7fcz]], [[7fd0]], [[7ydx]] – hRip1 catalytic domain + inhibitor
**[[6rln]], [[6ocq]], [[6nyh]], [[6hho]] – hRip1 catalytic domain (mutant) + inhibitor
**[[6ggs]] – hRip2 – Cryo EM
**[[5yrn]] – hRip2 CARD domain 434-540 – Cryo EM
**[[6szj]], [[6sze]], [[6s1f]], [[6rna]], [[6rn8]], [[6hmx]], [[6fu5]], [[6es0]], [[5w5o]], [[5w5j]] – hRip2 catalytic domain + inhibitor
**[[6ul8]] – hRip2 catalytic domain (mutant) + inhibitor
**[[8aza]] – hRip2 catalytic domain + XiaP Bir2 domain – Cryo EM
**[[7mx3]] – hRip3 catalytic domain (mutant) + inhibitor
**[[7mon]] – hRip3 catalytic domain (mutant) + MLKL
**[[7dac]] – hRip3 amyloid fibril - NMR
**[[7da4]] – hRip3 amyloid fibril – Cryo EM
**[[6oko]] – mRip3 catalytic domain + inhibitor
**[[6jpd]] – mRip3 residues 409-486 - NMR
**[[5wnm]], [[5wnj]] – mRip4 catalytic domain (mutant) + drug
**[[5wnl]] – mRip4 catalytic domain (mutant) + staurosporine
**[[5wnk]] – mRip4 catalytic domain (mutant) + inhibitor
**[[5wni]] – mRip4 catalytic domain (mutant) + ATP
**[[6gwm]] – rRip2 caspase recruitment domain 433-539
*'''Ulk'''
**[[6qas]] – hChk Ulk1 + inhibitor
**[[5ci7]], [[6mnh]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[8soi]], [[8sqz]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein
**[[8srm]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein – Cryo EM
**[[8srq]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein + PI3K – Cryo EM
**[[6qav]], [[6qau]], [[6qat]], [[6yid]] – hChk Ulk2 + inhibitor
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[6fdz]], [[6fdy]] – hChk Ulk3 + leukemia drug
**[[6tsz]] – hChk Ulk4 pseudfokinase domain + ATPgS
**[[6u5l]] – hChk Ulk4 (mutant) + inhibitor
*'''Hipa''' and '''Hipb'''
**[[3tpd]], [[3tpe]] – EcChk Hipa – ''Escherichia coli''
**[[3tpb]], [[3dnt]], [[3dnu]] – EcChk Hipa (mutant)
**[[4pu7]], [[4pu8]] – SoChk Hipb - ''Shewanella oneidensis''
**[[3tpt]] – EcChk Hipa (mutant) + ADP
**[[3fbr]] – EcChk Hipa (mutant) + AMPPNP + peptide
**[[3tpv]] – EcChk Hipa + ADP
**[[2wiu]] – EcChk Hipa + Hipb
**[[4yg7]], [[5k98]], [[3hzi]], [[3dnv]] – EcChk Hipa + Hipb + DNA
**[[4yg1]], [[4z58]], [[4z59]], [[4z5c]], [[4z5d]] – EcChk Hipb + DNA
**[[4z5h]] – EcChk Hipb (mutant) + DNA
**[[4pu3]], [[4pu4]] – SoChk Hipa + Hipb + DNA - ''Shewanella oneidensis''
**[[4pu5]] – SoChk Hipa + AMPPNP
*'''Chk Smg'''
**[[6l53]] – hChk Smg1 – Cryo EM
**[[7pw6]] – hChk Smg1 + inhibitor – Cryo EM
**[[7pw7]] – hChk Smg1 + Smg9 + inhibitor – Cryo EM
**[[7pw9]] – hChk Smg1 + Smg9 + AMPPNP + ATP – Cryo EM
**[[6l54]], [[6syt]] – hChk Smg1 + Smg8 + Smg9 – Cryo EM
**[[7pw4]], [[7pw5]] – hChk Smg1 + Smg8 + Smg9 + inhibitor – Cryo EM
**[[7pw8]] – hChk Smg1 + Smg8 + Smg9 + AMPPNP – Cryo EM
**[[6z3r]] – hChk Smg1 + Smg8 + Smg9 + regulator of nonsense transcripts – Cryo EM
**[[2hwy]] – hChk Smg5 PIN domain
**[[2hww]], [[2hwx]] – hChk Smg6 PIN domain (mutant)
**[[4um2]] – hChk Smg6 TPR domain
**[[1ya0]] – hChk Smg7 N terminal
*'''Chk Vprbp or DCAF1'''
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain 1039-1401 (mutant)
**[[7sse]], [[7ufv]], [[8f8e]], [[8og5]], [[8og6]], [[8og7]], [[8og8]], [[8og9]], [[8oga]], [[8ogb]], [[8ogc]], [[8oo5]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) + inhibitor
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[5aja]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
*'''Other Chk'''
**[[1wak]] – hChk Sprk1
**[[3dak]] – hChk Osr1 kinase domain
**[[7okw]] – hChk Osr1 C-terminal
**[[4aw2]] – hChk Mrckα kinase domain
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain (mutant)
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[1uf0]] – hChk Dcamkl1 DCX domain – NMR
**[[1u5q]] – rChk Tao2 kinase domain
**[[2cos]] – mChk Lats2 – NMR
**[[1xte]], [[1xtn]], [[6edx]] – mChk Sgk3 PX domain
**[[4yom]] – mChk Brsk2
**[[4ynz]] – mChk Brsk1 N terminal domain
**[[5iri]] – mChk Brsk1 residues 592-719
**[[5oat]], [[7mp8]] – rfbChk Pink1– red flour beetle
**[[7t3x]] – Chk Pink1 (mutant) – louse
**[[4f0g]] – smChk Roco4 kinase domain – slime mold
**[[5tos]] – AtChk Bik1
**[[1q8z]], [[1zyc]] – yChk
**[[1how]], [[1zxe]], [[1zy4]] – yChk (mutant)
**[[1ow5]], [[1x9x]] – yChk Ste11 SAM domain – NMR
**[[2kio]], [[2kit]], [[1w1n]] – yChk Tor1 FATC domain – NMR
**[[3gre]] – yChk Vps15 WD repeat domain
**[[3osm]], [[3ost]] - yChk Kcc4 kinase domain
**[[5yyx]] – yChk Mek1 FHA domain
**[[6jxc]], [[6jxa]] – yChk Tel1 – Cryo EM
**[[6u69]] – CaChk Yck2 – ''Candida albicans''
**[[6sl1]], [[6sl0]], [[6skz]], [[6sky]] – Chk Tel1 – ''Chaetonium thermophilum'' – Cryo EM
**[[6ra0]] – CeChk Dkf1 – ''Chaenorhabditis elegans''
**[[7z6e]] – CeChk Mrck1 regulatory domain
**[[6tlb]] – Chk – ''Plasmodium falciparum''
*Other Chk complexes
**[[1wbp]], [[7dd1]] – hChk Sprk1 + peptide
**[[3beg]] – hChk Srpk1 + splicing factor SF2
**[[3hdm]], [[3hdn]], [[7pue]] – hChk Sgk1 (mutant) + inhibitor
**[[2r5t]] – hChk Sgk3 + AMPPNP
**[[4yff]], [[4yfi]], [[6b5j]], [[7mgj]], [[7mgk]] – hChk Tnni3k + inhibitor
**[[2v3s]] – hChk Osr1 + hChk Wnk4 peptide
**[[2vwi]] – hChk Osr1 kinase domain + ANP
**[[7que]], [[7quf]] – hChk Drak1 kinase domain + inhibitor
**[[4crs]] – hChk N2 kinase domain + ATPγS
**[[3tku]], [[4ual]], [[3qfv]], [[5ote]], [[5otf]] – hChk Mrckβ + inhibitor
**[[4uak]] – hChk Mrckβ + ADP
**[[5aja]], [[4z8l]], [[4cc9]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
**[[5jk7]] – hChk Vprbp WD repeat domain + VPX + DDB1 + UDG
**[[3wa0]], [[4p7i]] – hChk Vprbp residues 1417-1506 + merlin
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[5ci7]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[5b5w]], [[5b6b]], [[5brk]] – hChk Lats1 residues 622-704 + MOB1
**[[5yz0]] – hChk Atr + Atr-interacting protein – Cryo EM
**[[6bdn]] – hChk Tao3 kinase domain + ADP
**[[5yh3]] – hChk Fam20C 141-578 + pseudokinase Fam20A
**[[2gcd]] – rChk Tao2 kinase domain + staurosporine
**[[1u5r]] – rChk Tao2 kinase domain + ATP
**[[5yj9]], [[7mp9]] – rfbChk Pink1 kinase domain + AMPPNP
**[[6bn1]] – DmChk Hippo SARAH domain + Shar-Pei
**[[3hgk]] – Chk Pto + effector protein AVRPTOB – Currant tomato
**[[3p86]], [[3ppz]] - AtChk Ctr1 + staurosporine
**[[4f0f]] – smChk Roco4 kinase domain + APPCP
**[[4f1m]], [[4f1o]] – smChk Roco4 kinase domain (mutant) + APPCP
**[[4f1t]], [[4yzm]], [[4yzn]] – smChk Roco4 kinase domain + inhibitor
**[[5fvm]] - Tor2 + LST8 - ''Kluyveromyces marxianus''
**[[5kc2]] - yVps15 + Vps34 - Cryo EM
**[[5dfz]] - yVps15 + Vps34 + Vps30 + VPSAP28 + VPSAP30 - Cryo EM
**[[1q8y]], [[1q97]], [[1q99]], [[1zyd]] – yChk + nucleotide
**[[1zy5]] – yChk (mutant) + nucleotide
**[[2jd5]] – yChk + NPL-3P
**[[4lqs]], [[4lqq]], [[4lqp]] – yChk Cbk1 residues 251-756 + Cbk1 activator Mob2
**[[6emk]] – yChk Tor2 + LST8 + TSC11 + AVO1 + AVO2 – Cryo EM
**[[6s8f]] – yChk Tel1 + AMPPNP – Cryo EM
**[[5yyz]] – yChk Mek1 FHA domain + Hop1
**[[5x6o]], [[6z3a]], [[7wzr]], [[7wzw]]– yChk Mec1 + LCD1 – Cryo EM
**[[6z2w]], [[6z2x]] – yChk Mec1 (mutant) + LCD1 – Cryo EM
**[[7kue]] – yChk Kin28 in TFIIK complex – Cryo EM
**[[6u6a]] – CaChk Yck2 + inhibitor
**[[5fvm]] – Chk Tor2 + LST8 – ''Kluyveromyces maximanus''
*Serine/threonine protein kinase Rad53 see [[Rad53]]
*Serine/threonine protein kinase Gsk3B see [[Glycogen synthase kinase 3]]
}}
[[Category:Topic Page]]

Serine/threonine protein kinase 3D structures

2026-08-19T07:20:02Z

Michal Harel:

==3D structures of serine/threonine protein kinase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Chk1'''; domains - kinase 1-289; KA1 393-492
**[[1ia8]] – hChk1 kinase domain – human
**[[5w12]] – hChk1 KA1 domain
**[[1zlt]] – hChk1 kinase domain + hymenaldisine
**[[1nvq]], [[1nvr]] – hChk1 kinase domain + peptide + saurosporine
**[[1nvs]], [[1zys]], [[7ako]] - hChk1 kinase domain + peptide + inhibitor
**[[7akm]] - hChk1 kinase domain + ATP
**[[2ayp]], [[2br1]], [[2brb]], [[2brg]], [[2brh]], [[2brm]], [[2brn]], [[2bro]], [[2c3j]], [[2c3k]], [[2c3l]], [[2cgu]], [[2cgv]], [[2cgw]], [[2cgx]], [[2e9n]], [[2e9o]], [[2e9p]], [[2e9u]], [[2e9v]], [[2gdo]], [[2ghg]], [[2hog]], [[2hxl]], [[2hxq]], [[2hy0]], [[2qhm]], [[2qhn]], [[2r0u]], [[3f9n]], [[2wmq]], [[2wmr]], [[2wms]], [[2wmt]], [[2wmu]], [[2wmv]], [[2wmw]], [[2wmx]], [[2xey]], [[2xf0]], [[2xez]], [[2x8d]], [[2x8e]], [[2x8i]], [[2ydi]], [[2ydj]], [[2ydk]], [[2yer]], [[2yex]], [[2ym3]], [[2ym4]], [[2ym5]], [[2ym6]], [[2ym7]], [[2ym8]], [[2ywp]], [[3jvr]], [[3jvs]], [[3nlb]], [[3ot3]], [[3ot8]], [[3pa3]], [[3pa4]], [[3pa5]], [[3tkh]], [[3tki]], [[3u9n]], [[4fsm]], [[4fsn]], [[4fsq]], [[4fsr]], [[4fst]], [[4fsu]], [[4fsw]], [[4fsy]], [[4fsz]], [[4ft0]], [[4ft3]], [[4ft5]], [[4ft7]], [[4ft9]], [[4fta]], [[4ftc]], [[4fti]], [[4ftj]], [[4ftk]], [[4ftl]], [[4ftm]], [[4ftn]], [[4fto]], [[4ftq]], [[4ftr]], [[4ftt]], [[4ftu]], [[4gh2]], [[4hyh]], [[4hyi]], [[4jik]], [[4qye]], [[4qyf]], [[4qyg]], [[4qyh]], [[4rvk]], [[4rvl]], [[4rvm]], [[5dls]], [[5f4n]], [[5fcf]], [[5fck]], [[6fc8]], [[6fcf]], [[6fck]], [[7bko]], [[8e80]], [[8e81]] - hChk1 kinase domain + inhibitor 
**[[5oot]], [[5op2]], [[5op4]], [[5op5]], [[5op7]], [[5opb]], [[5opr]], [[5ops]], [[5opu]], [[5opv]], [[5oq5]], [[5oq6]], [[5oq7]], [[5oq8]], [[7bjd]], [[7bjh]], [[7bjj]], [[7bjm]], [[7bjo]], [[7bjr]], [[7bjx]], [[7bk1]], [[7bk2]], [[7bk3]], [[7mck]], [[7suf]], [[7sug]], [[7suh]], [[7sui]], [[7suj]], [[8siv]], [[8siw]], [[8six]] - hChk1 kinase domain (mutant) + inhibitor
**[[5oop]] - hChk1 kinase domain (mutant) + AMPPNP
**[[5oor]] - hChk1 kinase domain (mutant) + staurosporine
**[[7bkn]] - hChk1 kinase domain + adenine
**[[7bje]] - hChk1 kinase domain (mutant) + adenine
**[[2jqi]] – yChk1 – yeast
*'''Chk2 (Checkpoint kinase)'''
**[[1gxc]] – hChk2 phosphothreonine-binding domain + phosphopeptide
**[[2cn5]] – hChk2 kinase domain + ADP
**[[2cn8]] – hChk2 kinase domain + inhibitor
**[[2w0j]], [[2w7x]], [[2wtc]], [[2wtd]], [[2xbj]], [[2xm8]], [[2xm9]], [[2yiq]], [[2yir]], [[2yit]], [[2cn8]], [[2ycf]], [[2ycq]], [[2ycr]], [[2ycs]], [[2wti]], [[2wtj]], [[2xk9]], [[4a9r]], [[4a9s]], [[4a9t]], [[4bda]], [[4bdb]], [[4bdc]], [[4bdd]], [[4bde]], [[4bdf]], [[4bdg]], [[4bdh]], [[4bdi]], [[4bdj]], [[4bdk]], [[2uv2]] - hChk2 kinase domain + inhibitor
**[[3i6u]], [[3i6w]] – hChk2 residues 84-502 (mutant)
*'''Chk3 (Mst2)'''; domains - kinase 13-313; SARAH 436-484
**[[4hkd]], [[4l0n]], [[4oh9]], [[3wws]] – hChk3 SARAH domain
**[[4lg4]] – hChk3 kinase domain
**[[4lgd]] – hChk3 kinase domain + RASSF5 SARAH domain
**[[6ao5]] – hChk3 kinase+SARAH domains (mutant) + SAV1 SARAH domain
**[[5dh3]], [[8a66]] – hChk3 kinase domain + inhibitor
*'''Chk4 (Mst1)''' ; Domains – kinase 1-311; SARAH 432-480
**[[3com]] – hChk4 kinase domain
**[[6yat]], [[8a5j]]– hChk4 kinase domain + inhibitor
**[[4nr2]] – hChk4 SARAH domain
**[[2jo8]] – hChk4 SARAH domain - NMR
**[[4oh8]] – hChk4 SARAH domain + Ras association domain-containing protein
*'''Chk5 (Aurora kinase b)'''
**[[4af3]] – hChk5 + inhibitor
*'''Chk6 or Chk15 or Aurora kinase A'''
**[[1muo]], [[1mq4]], [[4j8n]], [[6cpe]], [[4o0s]] – hChk6 kinase domain
**[[4bn1]], [[4o0w]], [[4o0u]] – hChk6 kinase domain (mutant)
**[[5dnr]], [[5drd]], [[5dt3]] – hChk6 kinase domain + ATP
**[[5drd]] – hChk6 kinase domain + ATP
**[[1ol6]] – hChk6 kinase domain (mutant) + ATP
**[[2wqe]] – hChk6 kinase domain (mutant) + ADP
**[[5odt]] – hChk6 kinase domain (mutant) + ADP + TACC3
**[[2c6d]] – hChk6 kinase domain (mutant) + ADPNP
**[[2dwb]] – hChk6 kinase domain + AMPPNP
**[[6cpf]] – hChk6 kinase domain + AMPPCP
**[[5g15]] – hChk6 kinase domain + AMPPNP + monobody
**[[6cpg]], [[8ssp]] – hChk6 kinase domain + inhibitor + monobody
**[[2j4z]], [[2j50]], [[2np8]], [[3efw]], [[2x81]], [[2x6d]], [[2x6e]], [[3myg]], [[3vap]], [[4b0g]], [[4j8m]], [[5dpv]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5one]], [[5obr]], [[4byi]], [[4byj]], [[4jai]], [[4jaj]], [[3w10]], [[3w16]], [[3w18]], [[3w2c]], [[4uzh]], [[4uzd]], [[4uyn]], [[4zs0]], [[4ztq]], [[4ztr]], [[4zts]], [[5aad]], [[5aae]], [[5aag]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5obr]], [[5one]], [[6gra]], [[6c2t]], [[6c2r]], [[5zan]], [[6z4y]], [[7ayh]], [[7ayi]], [[7fic]], [[7o2v]], [[8jmx]] – hChk6 kinase domain + inhibitor
**[[2bmc]], [[2c6e]], [[3coh]], [[3h0y]], [[3h0z]], [[3h10]], [[3fdn]], [[2wtw]], [[3lau]], [[3nrm]], [[2xne]], [[2xng]], [[2xru]], [[3k5u]], [[3m11]], [[3p9j]], [[3r21]], [[3r22]], [[3qbn]], [[3unz]], [[3uo4]], [[3uo5]], [[3uo6]], [[3uod]], [[3uoh]], [[3uoj]], [[3uok]], [[3uol]], [[3up2]], [[3up7]], [[4dhf]], [[4dea]], [[4deb]], [[4ded]], [[4dee]], [[5aad]], [[5aae]], [[5aaf]], [[5aag]], [[4jbo]], [[4jbp]], [[4jbq]], [[4prj]], [[5dpv]], [[6hjk]], [[6hjj]] – hChk6 kinase domain (mutant) + inhibitor
**[[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[5dos]], [[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5dn3]], [[5dos]], [[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor
**[[6c83]] – hChk6 kinase domain + AMPPCP + nanobody
**[[8sso]] – hChk6 kinase domain + drug + monobody
**[[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor
**[[5g1x]], [[7ztl]] – hChk6 kinase domain (mutant) + N-Myc
**[[8guw]] – hChk6 kinase domain/activator peptide
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + Targeting protein for XKLP2
**[[3daj]], [[3d14]], [[3dj5]], [[3dj6]], [[3dj7]], [[3d15]], [[3d2i]], [[3d2k]] – Chk6 kinase domain (mutant) + inhibitor - mouse
*Chk6 with phosphorylated Thr 287, Thr288
**[[1ol5]], [[1ol7]] – hChk6 kinase domain + PThr + ADP
**[[5dnr]], [[5dt3]] – hChk6 kinase domain + PThr + ATP
**[[2w1c]], [[2w1d]], [[2w1e]], [[2w1f]], [[2w1g]], [[5dn3]] – hChk6 kinase domain + PThr + inhibitor
**[[2wtv]], [[5orl]], [[5orn]], [[5oro]], [[5orp]], [[5orr]], [[5ors]], [[5ort]], [[5orv]], [[5orw]], [[5orx]], [[5ory]], [[5orz]], [[5os0]], [[5os1]], [[5os2]], [[5os3]], [[5os4]], [[5os5]], [[5os6]], [[5osd]], [[5ose]], [[5osf]] – hChk6 kinase domain (mutant) + PThr + inhibitor
**[[3e5a]], [[3ha6]] – hChk6 kinase domain + PThr + inhibitor + targeting protein for XKLP2
**[[5g1x]] – hChk6 kinase domain (mutant) + PThr + N-Myc
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + PThr + new antigen receptor variable domain
**[[5lxm]] – hChk6 kinase domain (mutant) + PThr + TPX2
**[[6r4d]], [[6r4c]], [[6r4b]], [[6r4a]] – hChk6 kinase domain + PThr + inhibitor + ADP
**[[6i2u]] – hChk6 kinase domain (mutant) + PThr + inhibitor + ADP
**[[6r49]] – hChk6 kinase domain (mutant) + PThr + CoA
*'''Chk10 (lymphocyte-oriented kinase)''' or LOK or STK10
**[[7qgp]] – hChk10
**[[2j7t]], [[4aot]], [[4equ]], [[4usd]], [[4use]], [[5ajq]], [[5owq]], [[5owr]], [[6eim]], [[6gtt]], [[6i2y]], [[6hxf]] – hChk10 kinase domain + inhibitor
**[[4bc6]], [[6i2y]] – hChk10 + drug
*'''Chk11'''
**[[2wtk]] – hChk11 (mutant) + calcium-binding protein
*'''Chk12-A (Aurora kinase b-a or Aurora B kinase)'''
**[[2vgo]], [[2vgp]], [[2vrx]], [[3ztx]], [[4c2v]], [[5eyk]] – fChk12-A + inner centromere protein A peptide + inhibitor - frog
**[[4c2w]] – fChk12-A + inner centromere protein A peptide + AMPPNP
**[[4b8l]], [[4b8m]], [[5k3y]] – fChk12-A (mutant) + inner centromere protein A peptide + inhibitor
*'''Chk13 (Polo-like kinase Plk)'''
*Plk1 Polo-box domain (Pbd) 371-594''
**[[1q4o]], [[2ogq]], [[3hih]], [[3p2w]], [[4h5x]], [[6n46]] – hPlk1 Pbd
*Plk1 Pbd complex with polypeptide
**[[1umw]], [[2ojx]], [[3bzi]], [[3c5l]], [[3rq7]], [[4dfw]], [[4whl]], [[4whk]], [[4whh]], [[4rcp]], [[4o6w]], [[4o56]], [[5dms]], [[5dmv]], [[5dnj]] , [[7mso]], [[7mx1]] – hPlk1 + peptide
**[[3hik]], [[3fvh]], [[3p2z]], [[3p34]], [[3p35]], [[3p36]], [[3p37]], [[3q1i]], [[4e67]], [[4e9c]], [[4e9d]], [[4hab]], [[4hy2]], [[4o9w]], [[4x9r]], [[4x9v]], [[4x9w]], [[5j19]], [[6gy2]] – hPlk1 + phosphopeptide
**[[1q4k]] – hPlk1 (mutant) + phosphopeptide
**[[2v5q]] – hPlk1 + design ankyrin repeat protein
**[[4lkl]] – hChk Plk1 + PL-55
**[[4lkm]] – hChk Plk1 + PL-74
**[[6ax4]] – hChk Plk1 + histidine cyclized macrocycle
**[[5x3s]] – mPlk1 + phosphopeptide
**[[8joq]], [[8joy]] – hPlk1 Pbd + hpv peptide
*Plk1 Pbd complex with small molecule inhibitor
**[[4h71]], [[4hco]], [[5ta6]], [[5ta8]], [[8bjt]], [[8crc]] – hPlk1 + inhibitor
**[[2rku]] – hPlk1 (mutant) + inhibitor
**[[3db6]], [[3db8]], [[3dbc]], [[3dbd]], [[3dbe]], [[3dbf]] – zfPlk1 (mutant) + inhibitor – zebra fish
*Plk1 catalytic domain 36-345
**[[2owb]] – hPlk1 catalytic domain (mutant)
**[[2ou7]] – hPlk1 catalytic domain (mutant) + AM
**[[3kb7]], [[2yac]], [[3thb]], [[4a4l]], [[4a4o]] – hPlk1 catalytic domain + inhibitor
**[[3fc2]] – hPlk1 catalytic domain (mutant) + inhibitor
**[[4j52]], [[4j53]] – hChk Plk1 (mutant) + inhibitor
**[[3d5x]] – zfPlk1 catalytic domain (mutant) + wortmannin
**[[3d5w]] – zfPlk1 catalytic domain + ADP
*'''Plk2'''
**[[4i5m]], [[4i5p]], [[4i6b]], [[4i6f]], [[4i6h]] – hChk Plk2 kinase domain (mutant) + inhibitor
**[[4xb0]], [[4rs6]] – hChk Plk2 Pbd
*'''Plk3'''
**[[4b6l]], [[4i6b]] – hChk Plk3 kinase domain + inhibitor
*'''Plk4'''; Domains – kinase 2-275; Pbd 580-808; Pb3 884-970
**[[3cok]] – hChk Plk4 kinase domain
**[[4n9j]] – hChk Plk4 Pbd domain
**[[4n7z]], [[4n7v]] – hChk Plk4 Pbd domain + centrosomal protein
**[[6w38]], [[6w3i]] – hChk Plk4 Pbd domain + Fam46C
**[[6w3j]] – hChk Plk4 Pbd domain + Fam46C + CEP92 peptide
**[[4jxf]], [[4yur]] – hChk Plk4 kinase domain + inhibitor
**[[5lhy]] – hChk Plk4 Pb3 domain
**[[4yyp]], [[5lhz]] – hChk Plk4 Pb3 domain + Scl-interrupting locus protein
**[[4nk7]], [[4g7n]], [[5lhx]], [[7rl3]] – DmChk Plk4 Pbd domain – ''Drosophila melanogaster''
*'''Chk16'''
**[[2buj]] – hChk16 (mutant) + staurosporin
*'''Chk17B''' or DRAK2 or STK17B
**[[3lm0]] – hChk17B
**[[6qf4]], [[7q7c]], [[7q7d]] – hChk17B + ADP
**[[7q7e]] – hChk17B + ATP
**[[3lm5]] – hChk17B + quercetin
**[[6y6f]], [[6y6h]], [[6zjf]] – hChk17B + pyrimidine derivative
**[[7akg]] – hChk17B + drug
*'''Chk19''' or STK19
**[[7xrb]] – hChk19
*'''Chk24 (Mst3)''' or STK24
**[[3a7f]], [[3a7g]], [[3a7h]], [[3a7i]], [[3a7j]], [[3ckw]] – hChk24 kinase domain
**[[4w8e]], [[4w8d]], [[4u8z]], [[4qmm]], [[4qmn]], [[4qmo]], [[4qmp]], [[4qmq]], [[4qms]], [[4qmt]], [[4qmu]], [[4qmv]], [[4qmw]], [[4qmx]], [[4qmy]], [[4qmz]], [[4qna]], [[4qo9]], [[4u8z]], [[7b30]], [[7b31]], [[7b32]], [[7b33]], [[7b34]], [[7b35]], [[8bzi]], [[8bzj]], [[8qlr]], [[8qls]], [[8qlt]] – hChk Mst3 + inhibitor
**[[8qlq]] – hChk Mst3 + macrocyclic inhibitor
**[[3ckx]] – hChk24 kinase domain + staurosporin
**[[3zhp]] – hChk24 kinase domain + calcium-binding protein
**[[4o27]] – hChk24 kinase domain (mutant) + calcium-binding protein
**[[4qml]] – hChk Mst3 kinase domain + AMPPNP
*'''Chk25 or STK25'''
**[[2xik]] – hChk25 kinase domain
**[[7z4v]] – hChk25 kinase domain + inhibitor
**[[3w8h]] – hChk25 regulatory domain + programmed cell death protein 10
**[[4nzw]] – hChk25 kinase domain (mutant) + calcium-binding protein
*'''Chk26 (Mst4)'''
**[[3ggf]], [[7b36]] – hChk Mst4 + inhibitor
**[[4geh]], [[3w8i]] - hChk Mst4 dimerization domain + programmed cell death protein 10
**[[4fza]], [[4fzd]], [[4fzf]] – hChk Mst4 (mutant) + calcium-binding protein
*'''Chk32'''
**[[4fr4]] – hChk32A
*'''Chk38'''
**[[6bxi]] – hChk38 kinase domain
*'''Chk39''' or SPAK
**[[7o86]] – hChk39 C-terminal
**[[5d9h]] – mChk39 residues 63-403 + ATP
**[[5dbx]] – mChk39 residues 63-403 (mutant) + AMPPNP
*'''Chk40'''
**[[5l2q]] – hChk40 kinase homology domain
*'''Dclk1'''
**[[6kyq]] – hChk Dclk1 kinase domain
**[[6kyr]] – hChk Dclk1 kinase domain (mutant)
**[[5jzj]] – hChk Dclk1 kinase domain + AMPPN
**[[5jzn]], [[7kx6]], [[7kxw]] – hChk Dclk1 kinase domain + inhibitor
**[[7f3g]] – hChk Dclk1 kinase domain + drug
**[[7kx8]] – hChk Dclk1 C-terminal + inhibitor
*'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123; kinase 144-480
**[[1unp]], [[1unr]] – hRac-α hChk pleckstrin homology domain
**[[2uzr]], [[2uzs]], [[7myx]] – hRac-α hChk pleckstrin homology domain (mutant)
**[[1h10]], [[1unq]], [[2uvm]] – hRac-α hChk pleckstrin homology domain + inositol tetrakisphosphate
**[[3o96]], [[4ejn]], [[6s9w]], [[6s9x]], [[6hhj]], [[6hhi]], [[6hhh]], [[6hhg]], [[6hhf]] - hRac-α hChk + inhibitor
**[[5kcv]], [[7nh4]], [[7nh5]] - hRac-α hChk (mutant) + inhibitor
**[[4gv1]], [[4ekl]] - hRac-α hChk kinase domain + inhibitor
**[[3qkm]], [[6ccy]] - hRac-α hChk kinase domain (mutant) + inhibitor
**[[6buu]] - hRac-α hChk kinase domain + bisubstrate peptide
**[[4ekk]] - hRac-α hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[6npz]] - hRac-α hChk kinase domain + peptide + inhibitor
**[[3ow4]], [[3qkk]], [[3qkl]], [[6buu]] - hRac-α hChk kinase domain (mutant) + peptide + inhibitor
**[[7apj]] - hRac-α hChk + nanobody
*'''Rac-β hChk (AKT2)'''
**[[1gzk]], [[1gzn]], [[1gzo]], [[1mrv]], [[1mry]] – hRac-β hChk kinase domain
**[[1p6s]] - hRac-β hChk pleckstrin homology domain - NMR
**[[1o6k]] - hRac-β hChk kinase domain + GSK3 peptide + AMPPNP
**[[2jdo]], [[2jdr]], [[2uw9]], [[2x39]], [[3cqu]], [[3cqw]] - hRac-β hChk kinase domain + GSK3 peptide + inhibitor
**[[3e87]], [[3e88]], [[3e8d]] - Rac-β hChk kinase domain (mutant) + GSK3 peptide + inhibitor<br /
**[[1o6l]] - hRac-β hChk kinase domain (mutant) + GSK3 peptide + AMPPNP
**[[3d0e]], [[8q61]] - hRac-β hChk kinase domain (mutant) + inhibitor
*'''Rac-γ hChk (ATK3)'''
**[[2x18]] – Rac-γ hChk PH domain
*'''A-Raf'''
**[[1wxm]] – hA-Raf RAS-binding domain 19-91 - NMR
**[[2mse]] – hA-Raf RAS-binding domain + APOA-I + K-ras - NMR
*'''B-Raf'''; domains - BRS 38-116; Ras-binding 153-237; kinase 445-723
**[[8dgs]], [[8dgt]] – hB-Raf in Ras/Raf complex – Cryo EM
**[[7z37]], [[7z38]], [[7zr5]] – hB-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
**[[1uwh]], [[3c4c]], [[6v2u]], [[6xfp]], [[6xlo]], [[8f7o]], [[8f7p]] – hB-Raf kinase domain + anticancer drug
**[[1uwj]], [[6p3d]] – hB-Raf kinase domain (mutant) + anticancer drug
**[[2fb8]], [[3d4q]], [[3ii5]], [[3psd]], [[3skc]], [[3tv6]], [[4g9c]], [[4ksp]], [[4ksq]], [[3psb]], [[3ppj]], [[3ppk]], [[3prf]], [[3pri]], [[3tv4]], [[4dbn]], [[4e4x]], [[4mbj]], [[4ehe]], [[3q4c]], [[3q96]], [[3e26]], [[4h58]], [[4e26]], [[4fc0]], [[4pp7]], [[6cad]], [[7shv]] – hB-Raf kinase domain + pyrazole inhibitor
**[[4jvg]], [[4ehg]], [[4fk3]], [[3idp]], [[4g9r]], [[4wo5]], [[4mnf]], [[4r5y]], [[4rzv]], [[4rzw]], [[4xv1]], [[4xv2]], [[4xv3]], [[4xv9]], [[4yht]], [[5c9c]], [[5hi2]], [[5ita]], [[5jrq]], [[5jsm]], [[5jt2]], [[6nsq]], [[6p7d]], [[6uuo]] – hB-Raf kinase domain (mutant) + pyrazole inhibitor
**[[5csw]], [[5csx]], [[5ct7]], [[5fd2]], [[5hid]], [[5hie]], [[5val]], [[5vam]], [[6b8u]], [[6n0q]], [[6n0p]], [[7k0v]], [[7p3b]], [[7p3v]], [[8c7x]], [[8c7y]] - hB-Raf kinase domain + inhibitor
**[[6v34]] – hB-Raf kinase domain (mutant) + inhibitor
**[[4mne]] – hB-Raf kinase domain + MAPKK1
**[[8f7o]] – hB-Raf kinase domain + drug
**[[7m0u]] – hB-Raf kinase domain + AMPPNP + drug
**[[6u2h]] – hB-Raf kinase domain + 14-3-3 ζ/δ
**[[7mfe]] – hB-Raf + 14-3-3 ζ/δ – Cryo EM
**[[7mff]] – hB-Raf + 14-3-3 ζ/δ + inhibitor – Cryo EM
**[[7mfd]] – hB-Raf + 14-3-3 ζ/δ + MEK + inhibitor – Cryo EM
**[[6pp9]] – hB-Raf kinase domain + MEK1 + ANP
**[[7m0x]], [[7m0z]] – hB-Raf kinase domain + MEK1 + ANP + inhibitor
**[[7m0t]], [[7m0u]], [[7m0v]], [[7m0w]], [[7m0y]] – hB-Raf kinase domain + MEK1 + ANP + drug
**[[6u2g]] – hB-Raf kinase domain + MEK1 + AMPPCP
**[[5vr3]] – hB-Raf BRS domain
**[[7jhp]] – hB-Raf BRS domain + Hras
**[[6ntc]], [[6ntd]] – hB-Raf BRS domain (mutant) + Hras
**[[6xi7]] – hB-Raf 52-188 + Kras
**[[2l05]], [[5j17]], [[5j2r]] – hB-Raf RAS-binding domain - NMR
**[[3ny5]] – hB-Raf RAS-binding domain
**[[5j18]] – hB-Raf RAS-binding domain + inhibitor - NMR
**[[6pts]], [[6ptw]] – hB-Raf 56-187 + Kras + apolipoprotein + GMPPNP - NMR
**[[6uan]], [[6q0k]] – hB-Raf + 14-3-3 ζ – Cryo EM
**[[6nyb]] – hB-Raf + 14-3-3 ζ + MEK1 – Cryo EM
**[[6q0t]], [[6q0j]] – hB-Raf (mutant) + 14-3-3 ζ + MEK1 – Cryo EM
*'''c-Raf'''; Domains – RAS-binding (RBD) 55-132; Cys-rich 136-187 (CBD); kinase 323-618
**[[1rfa]], [[8jna]], [[8jof]], [[8jog]] – hc-Raf RBD - NMR
**[[1faq]], [[1far]] – hc-Raf cysteine-rich domain - NMR
**[[3omv]] – hc-Raf kinase domain
**[[1rrb]] – c-Raf RBD – NMR - rat
*c-Raf complex with protein
**[[8cpd]] – hc-Raf + 14-3-3 protein zeta – Cryo EM
**[[9mmp]] – hc-Raf + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[9mmr]] – hc-Raf (mutant) + MEK1 + 14-3-3 protein zeta – Cryo EM
**[[1c1y]] – hc-Raf RBD + RAP1A
**[[3kuc]] – hc-Raf RBD (mutant) + RAP1A
**[[1gua]] – hc-Raf RBD + RAP1A + GPPNHP
**[[8jnb]] – hc-Raf RBD + ligand
**[[4g0n]], [[4g3x]] – hc-Raf RBD + GTPase Hras
**[[3kud]] – hc-Raf RBD (mutant) + GTPase Hras
**[[8epw]], [[8t74]] – hc-Raf RBD + GTPase K-ras
**[[8t75]], [[9ygs]] – hc-Raf RBD-CRD + GTPase K-ras + GMPPNP
**[[9ay7]], [[9aya]] – hc-Raf + MEK1
**[[9mmq]] – hc-Raf + MEK1 – Cryo EM
**[[9mms]] – hc-Raf (mutant) + MEK1 – Cryo EM
**[[9o0u]], [[9o0v]] – hc-Raf (mutant) + MEK1 + ANP + inhibitor– Cryo EM
**[[8u1l]] – hc-Raf + Hsp90 + CDC37 – Cryo EM
**[[8gae]], [[8gft]] – hc-Raf + Hsp90 + CDC37 + PP5 – Cryo EM
*'''Snf1-related Chk'''
**[[3uc4]], [[3uc3]], [[3udb]], [[3zut]], [[3zuu]] – AtChk Srk2E kinase domain (mutant) – ''Arabidopsis thaliana''
**[[3ujg]] – AtChk Srk2E kinase domain (mutant) + protein phosphatase 2C
**[[5yks]] – hChk
*'''MAPK-interacting Chk''' or Mnk1 Mnk2
**[[2hw6]] – hMnk 1 catalytic domain
**[[2hw7]] – hMnk 1 catalytic domain + staurosporin
**[[5wvd]] – hMnk 1 catalytic domain + inhibitor
**[[2ac3]] – hMnk 2 catalytic domain
**[[2ac5]] – hMnk 2 catalytic domain (mutant)
**[[6cj5]], [[6cje]], [[6cjh]], [[6cjw]], [[6cjy]], [[6ck3]], [[6ck6]], [[6cki]] – hMnk 2 catalytic domain (mutant) + inhibitor
*'''hChk Pak''' or '''Chk N''' or '''PRK1'''; Domains - CRIB 74-109; Hr1B 122-199; catalytic 109-426; kinase 605-942
**[[1urf]] – hChk Pak-1 Hr1b domain - NMR
**[[4nkg]] – hChk Pak-1 Hr1b domain + SSPH1 LRR domain
**[[2rmk]] – hChk Pak-1 Hr1bb domain + Rac1 - NMR
**[[1f3m]] – hChk Pak-1 autoregulatory+kinase domains
**[[4otd]] - hChk Pak-1 kinase domain
**[[1yhv]], [[1yhw]], [[3q4z]], [[3q52]], [[3q53]] – hChk Pak-1 kinase domain (mutant)
**[[4o0r]], [[4o0t]], [[4zji]], [[4zjj]], [[4zlo]], [[4zy4]], [[4zy5]], [[4zy7]], [[5ime]], [[5kbq]], [[5kbr]], [[6b16]], [[7vto]] – hChk Pak-1 kinase domain + inhibitor
**[[4oti]], [[4oth]], [[4otg]] – hChk Pak-1 kinase domain + inhibitor
**[[4eqc]], [[4p90]], [[5dew]], [[5dey]], [[5dfp]] – hChk Pak-1 kinase domain (mutant) + inhibitor
**[[2hy8]] – hChk Pak-1 kinase domain + staurosporin
**[[2qme]] – hChk Pak-1 CRIB domain + RAC3
**[[3fxz]], [[3fy0]], [[4daw]] – hChk Pak-1 kinase domain (mutant) + Ru complex
**[[6fd3]] – hChk Pak-3 kinase domain (mutant)
**[[2j0i]], [[4fie]] – hChk Pak-4
**[[4fig]], [[4fij]], [[4l67]] – hChk Pak-4 kinase domain
**[[2cdz]] – hChk Pak-4 + purine derivative
**[[2ov2]] – hChk Pak-4 CRIB domain + RAC3
**[[2qon]], [[4fif]], [[4fih]], [[4fii]], [[4jdh]], [[4jdi]], [[4jdj]], [[4jdk]], [[6wlx]], [[6wly]] – hChk Pak-4 kinase domain + peptide
**[[4app]], [[4o0v]], [[4o0x]], [[4o0y]], [[4njd]], [[4xbu]], [[5bms]], [[5i0b]], [[5vee]], [[5vef]], [[5zjw]], [[5xvg]], [[5xvf]], [[5xva]], [[7cmb]], [[7cp3]], [[7cp4]] – hChk Pak-4 kinase domain + inhibitor
**[[2x4z]], [[2xh5]] – hChk Pak-4 kinase domain (mutant) + inhibitor
**[[5upl]], [[5upk]] – hChk Pak-4 kinase domain (mutant) + CDC42
**[[5ved]] – hChk Pak-4 kinase domain + staurosporine
**[[8ahi]] – hChk Pak-4 300-591 + inhibitor
**[[7s46]], [[7s48]] – hChk Pak-4 catalytic domain + integrin beta-5 peptide
**[[2c30]] – hChk Pak-6
**[[2odb]] – hChk Pak-6 CRIB domain + CDC42
**[[4ks8]] – hChk Pak-6 kinase domain + sunitinib
**[[4ks7]] – hChk Pak-6 kinase domain (mutant) + inhibitor
**[[2f57]] – hChk Pak-7
*'''Mycobacterium tuberculosis Chk Pkn'''
**[[4x3f]] - MtChk PknA – ''Mycobacterium tuberculosis''
**[[4ow8]] - MtChk PknA kinase domain
**[[3ori]], [[3ork]], [[3orl]], [[3orm]], [[3oro]], [[3orp]], [[3ort]] - MtChk PknB kinase domain (mutant)
**[[1o6y]] – MtChk PknB kinase domain
**[[6b2p]], [[6b2q]] – MtChk PknB kinase domain + inhibitor
**[[2kud]], [[2kue]], [[2kuf]], [[2kui]] – MtChk PknB pasta domains 2-3 - NMR
**[[3ouv]] – MtChk PknB pasta domain 3
**[[5e0y]] – MtChk PknB pasta domain 4
**[[5e10]] – MtChk PknB pasta domains 1-2
**[[5e0z]] – MtChk PknB pasta domains 3-4
**[[5e12]] – MtChk PknB pasta domains 2-4
**[[5u94]] - MtChk PknB kinase domain + inhibitor
**[[3f61]], [[3f69]] - MtChk PknB kinase domain (mutant) + inhibitor
**[[6i2p]] - MtChk PknB kinase domain (mutant) + GARA + peptide
**[[1rwi]], [[1rwl]] - MtChk PknD extracellular domain
**[[2h34]] – MtChk PknE catalytic domain
**[[7naa]] – MtChk PknF kinase domain + inhibitor
**[[4y12]] - MtChk PknG + ATP-gS
**[[4y0x]] - MtChk PknG + ADP
**[[7q52]] - MtChk PknG + inhibitor
**[[4esq]] - MtChk PknH extracellular domain
**[[5m06]], [[5xka]] - MtChk PknI kinase domain
**[[5m07]], [[5m08]], [[5m09]] - MtChk PknI kinase domain (mutant)
**[[5xlm]], [[5xll]] - MtChk PknI sensor domain
**[[7mxb]], [[7mxj]], [[7mxk]] - Chk PknG kinase domain + AMPPNP - Corynebacterium glutamicum
*'''hChk Nek'''
**[[4apc]] – hChk Nek1 kinase domain (mutant)
**[[4b9d]] - hChk Nek1 kinase domain (mutant) + inhibitor
**[[2w5h]] – hChk Nek2 kinase domain
**[[2jav]], [[2wqo]], [[2xk3]], [[2xk4]], [[2xk6]], [[2xk7]], [[2xk8]], [[2xkc]], [[2xkd]], [[2xke]], [[2xkf]], [[2xnm]], [[2xnn]], [[2xno]], [[2xnp]], [[4a4x]], [[4afe]], [[5m51]], [[5m53]], [[5m55]], [[5m57]], [[6sgd]], [[6sgh]], [[6sgi]], [[6sgk]], [[6sk9]] – hChk Nek2 + inhibitor
**[[2w5a]], [[2w5b]] – hChk Nek2 + nucleotide
**[[6tm5]] - hChk Nek2 in anaphase-promoting complex – Cryo EM
**[[2wqm]], [[6s76]] – hChk Nek7
**[[2wqn]] – hChk Nek7 + ADP
**[[5de2]] – hChk Nek7 + hChk Nek9
**[[6s73]], [[2wqo]] – hChk Nek7 + inhibitor
**[[6npy]] – hChk Nek7 + Nlrp3
**[[6s75]] – hChk Nek7 + inhibitor
*'''Chk Rio'''
**[[6fdo]], [[6fdn]], [[6fdm]] – hChk Rio2
**[[4otp]] – hChk Rio1 Rio domain + ADP
**[[6hk6]], [[7vbt]] – hChk Rio2 + inhibitor
**[[6eml]], [[6fai]], [[6g18]], [[6g51]], [[6rbd]],[[6rbe]], [[6y7c]] – yChk Rio2 in 40S particle – Cryo EM
**[[1ztf]] – AfChk Rio1 + adenine derivative – Archaeoglobus fulgidus
**[[1zth]] – AfChk Rio1 + ADP
**[[1zp9]] – AfChk Rio1 + ATP
**[[1tqp]], [[1zao]] – AfChk Rio2 + ATP
**[[1zar]] – AfChk Rio2 + ADP
**[[4gyg]] – CtChk Rio2 – Chaetonium thermophilum
**[[4gyi]] – CtChk Rio2 + ADP
*hChk Vrk (vaccinia-related kinase)
**[[2kty]], [[2kul]], [[2lav]], [[2rsv]] – hChk Vrk1 kinase domain 1-396 - NMR
**[[3op5]] – hChk Vrk1 kinase domain (mutant)
**[[5ukf]] – hChk Vrk1 kinase domain + inhibitor
**[[5uvf]], [[6cnx]], [[6bu6]], [[6cfm]], [[6dd4]], [[6bp0]], [[6bru]], [[6btw]], [[6cmm]], [[6cqh]], [[6csw]], [[6npn]], [[6vxu]], [[6vzh]] – hChk Vrk1 kinase domain (mutant) + inhibitor
**[[6ac9]] – hChk Vrk1 kinase domain (mutant) + AMPPNP
**[[7tan]] – hChk Vrk1 kinase domain + nucleosome – Cryo EM
**[[2v62]] – hChk Vrk2 kinase domain
**[[5uu1]], [[6ncg]], [[8q1z]] – hChk Vrk2 kinase domain + inhibitor
*Chk Wnk (protein kinase lysine-deficient); Domains - kinase 194-483; CCT1 454-549
**[[6cn9]], [[4q2a]], [[4pwn]] - hChk Wnk1 kinase domain (mutant)
**[[5tf9]] - hChk Wnk1 kinase domain + inhibitor + AMPPNP
**[[5wdy]], [[5we8]] - hChk Wnk1 kinase domain + inhibitor + ANP
**[[5drb]], [[6ol2]]- rChk Wnk1 kinase domain (mutant) + inhibitor
**[[6elm]] - hChk Wnk2 CCT1 domain
**[[6fbk]] - hChk Wnk2 CCT1 domain + Wnk1 peptide
**[[5o1v]], [[5o21]], [[5o23]] - hChk Wnk3 kinase domain
**[[5o2c]] - hChk Wnk3 kinase + CCT1 domains
**[[5o26]], [[5tf9]] - hChk Wnk3 kinase domain + AMPPNP
**[[5o2b]] - hChk Wnk3 kinase domain + inhibitor
**[[8edh]] - hChk Wnk3 kinase domain (mutant) + inhibitor
**[[2lru]] – rChk Wnk1 autoinhibitory domain 480-572 - NMR
**[[5w7t]] - rChk Wnk1 kinase domain
**[[7uos]] - rChk Wnk1 kinase domain (mutant)
*'''TANK-binding kinase'''
**[[4efo]] – hChk Tbk1 ubiquitin-like domain
**[[6rsr]], [[6rsu]] – hChk Tbk1 + inhibitor
**[[4im0]], [[4im2]], [[4im3]], [[4iw0]], [[4iwo]], [[4iwp]], [[4ipq]], [[6rst]] – hChk Tbk1 (mutant) + inhibitor
**[[6cq5]], [[6cq4]], [[6cq0]], [[6boe]], [[6bod]], [[6bny]], [[5w5v]] – hChk Tbk1 + ulcer drug
**[[4eut]], [[4euu]] – hChk Tbk1 kinase+ubiquitin-like domains (mutant) + inhibitor
**[[6nt9]] – hChk Tbk1 (mutant) + STING
**[[5eoa]], [[5eof]] – hChk Tbk1 residues 677-729 + optineurin
**[[4jl9]], [[4jlc]] – mChk Tbk1 + inhibitor
**[[6o8c]], [[6o8b]] – mChk Tbk1 (mutant) + STING
*'''Haspin'''
**[[2vuw]], [[2wb8]] – hChk Haspin kinase domain
**[[3dle]] – hChk Haspin kinase domain + AMP
**[[3e7v]], [[3f2n]], [[3fmd]], [[3iq7]], [[4qtc]], [[5htb]], [[5htc]], [[6z56]], [[6z57]], [[6z58]], [[6z59]], [[6z5a]], [[6z5b]], [[6z5c]]. [[6z5d]], [[6z5e]] , [[7avq]], [[7ops]] – hChk Haspin kinase domain + inhibitor
**[[7sqm]] – hChk Haspin kinase domain + antimalarial
**[[6g38]], [[6g34]], [[6g35]], [[6g36]], [[6g37]] – hChk Haspin kinase domain + tubercidin derivative
**[[6g39]], [[6g3a]] – hChk Haspin kinase domain (mutant) + tubercidin derivative
**[[4ouc]] – hChk Haspin kinase domain + histone H3 peptide
*'''MAP/microtubule affinity-regulating kinase (MARK)'''
**[[2hak]] – hChk MARK1 catalytic+UBA domains
**[[3ose]] - hChk MARK1 KA1 domain
**[[6c9d]] – hChk MARK1 catalytic+UBA+KA1 domains (mutant)
**[[5eak]], [[5kz7]], [[5kz8]] – hChk MARK2 catalytic+UBA domains + inhibitor
**[[3iec]] – hChk MARK2 catalytic+UBA domains + cytotoxicity-associated immunodominant antigen peptide
**[[2qnj]] – hChk MARK3 catalytic+UBA domains
**[[3fe3]] – hChk MARK3 catalytic+UBA domains (mutant)
**[[7p1l]] – hChk MARK3 catalytic+UBA domains + inhibitor
**[[5es1]] – hChk MARK4 catalytic+UBA domains + inhibitor
**[[1zmu]] – rChk MARK2 catalytic+UBA domains
**[[2wzj]], [[2r0i]], [[1zmv]], [[1y8g]], [[1zmw]] – rChk MARK2 catalytic+UBA domains (mutant)
**[[1ul7]], [[1v5s]] - mChk MARK3 catalytic domain - NMR
*'''Mitotic checkpoint Chk (Bub)'''; Domains: TPR 1-220; kinase 726-1085
**[[2lah]] – hChk Bub1 TPR domain – NMR
**[[2wvi]] – hChk Bub1β TPR domain
**[[3si5]] – hChk Bub1 TPR domain + CASC5 peptide
**[[4r8q]], [[4qpm]], [[5dmz]] – hChk Bub1 kinase domain + ADP
**[[6f7b]] – hChk Bub1 kinase domain + inhibitor
**[[4a1g]] – hChk Bub1 TPR domain + CASC5 KI motif
**[[4ggd]] - hChk Bub1 + cell division cycle protein
**[[6tlj]], [[5khu]] - hChk Bub1 in anaphase-promoting complex – Cryo EM
**[[6jkk]] – DmChk Bub1 kinase domain
**[[6jkm]] – DmChk Bub1 kinase domain + ADP
**[[5jja]] – hChk Bub1 residues 661-734 + PP2A
**[[3esl]] – yChk Bub1 N terminal
**[[4bl0]] - yChk Bub1 + cell cycle arrest protein Bub3
*'''Microtubule-associated Chk'''
**[[2m9x]] – hChk 1 residues 187-287 – NMR
**[[3ps4]] - hChk 1 residues 965-1057
**[[2kqf]], [[2kyl]] – hChk 2 PDZ domain + glycoprotein C terminal – NMR
**[[3khf]] - hChk 3 PDZ domain
**[[2w7r]] – hChk 4 PDZ domain
*'''mTOR''' or '''Mechanistic target of rapamycin'''
*''mTOR FRB domain residues 2015-2114''
**[[1nsg]], [[1fap]] – hFRAP FRB domain + FKBP
**[[2rse]] – hFRAP FRB domain + FKBP – NMR
**[[1aue]] – hFRAP FRB domain
**[[2gaq]], [[2npu]] – hFRAP FRB domain - NMR
**[[8ppz]] – hFRAP FRB domain + FKBP + pyridine derivative
**[[3fap]], [[2fap]], [[4fap]] – hFRAP FRB domain + FKBP + rapamycin analog
**[[4drh]], [[4dri]], [[4drj]], [[5gpg]] – hFRAP FRB domain + FKBP + rapamycin
**[[6m4u]], [[6m4w]] – hChk Mtor FRB domain (mutant) + FKBP1A + rapamycin
**[[5wbh]] – hFRAP FRB domain + S6K1 peptide
*''mTOR FAT+PIKK domain residues 1376-2549''
**[[4jsn]] – hFRAP + TORC subunit LST8
**[[4jsp]] – hFRAP + TORC subunit LST8 + ATP
**[[4jsv]] – hFRAP + TORC subunit LST8 + ADP
**[[4jsx]] – hFRAP + TORC subunit LST8 + torin2
**[[4jt5]] – hFRAP + TORC subunit LST8 + pp242
**[[4jt6]] – hFRAP + TORC subunit LST8 + PI-103
**[[5wby]], [[5wbu]] – hFRAP + TORC subunit LST8 + proline-rich Akt1 substrate
*''mTOR complex''
**[[5flc]] – hmTOR + RAPTOR + LST8 + FKBP – Cryo EM
**[[5h64]] – hmTOR + RAPTOR + LST8 – Cryo EM
**[[6sb2]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC – Cryo EM
**[[6sb0]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC + proline-rich Akt1 substrate – Cryo EM
**[[5zcs]] – hmTOR + LST8 + AVO3 + TORC2 – Cryo EM
**[[7tzo]] – hTORC2 in mTORC2 complex– Cryo EM
**[[6zwm]], [[6zwo]], [[7owg]], [[7pe7]], [[7pe8]], [[7pe9]], [[7pea]], [[7peb]], [[7pec]], [[7uxc]] , [[8era]]– mTOR in mTor complex – Cryo EM
*'''Gcn2'''
**[[1zyc]] – yChk Gcn2
**[[1zxe]], [[1zy4]], [[1zy5]] – yChk Gcn2 (mutant)
**[[2yz0]] – yChk Gcn2 RWD/GI domain – NMR
**[[4otm]] – yChk Gcn2 C terminal domain
**[[1zyd]] – yChk Gcn2 + ATP
**[[4otn]] – mChk Gcn2 C terminal domain
*'''LRRK1''' or leucine-rich repeat Chk1
**[[8e04]], [[8e05]], [[8e06]], [[8fac]] – hLRRK1 – Cryo EM
*'''LRRK2''' or leucine-rich repeat Chk2 or dardarin
**[[6xr4]] – hLRRK2 – Cryo EM
**[[7lht]], [[7lhw]], [[7li4]] – hLRRK2 + ATP + GDP – Cryo EM
**[[7li3]] – hLRRK2 (mutant) + ATP + GDP – Cryo EM
**[[6oje]], [[7thy]] – hLRRK2 GTPase domain 1329-1520
**[[6ojf]] – hLRRK2 GTPase domain (mutant)
**[[6dlo]], [[6dlp]] – hLRRK2 WD40 domain
**[[7thz]] – hLRRK2 1330-1527 + GDP
**[[6vno]], [[6vp6]], [[6vp7]] – hLRRK2 C terminal 1330-2527 – Cryo EM
**[[6vp8]] – hLRRK2 C terminal 1330-2527 + COR domain 1670-1950 + WD40 domain 2140-2489 – Cryo EM
**[[6s6q]] – AtLRRK2 ectodomain + protein casparian strip peptide
*'''Pim'''
*Pim1 catalytic domain residues 14-313
**[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain
**[[1yxs]] – hPim1 catalytic domain (mutant)
**[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP
**[[1yxu]] – hPim1 catalytic domain + AMP
**[[1yxv]], [[5ipj]] – hPim1 catalytic domain + quinoline derivative
**[[1yxx]] – hPim1 catalytic domain + indole derivative
**[[2bzh]], [[2bzi]], [[2bzj]] – hPim1 catalytic domain (mutant) + organometallic ligand
**[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3c4e]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umw]], [[3umx]], [[4enx]], [[4eny]], [[4k1b]], [[4k18]], [[4k0y]], [[4iaa]], [[4i41]], [[4ll5]], [[4lm5]], [[4lmu]], [[4mta]], [[4med]], [[4mbl]], [[4mbi]], [[4n6y]], [[4n6z]], [[4n70]], [[4xh6]], [[5iis]], [[5kgd]], [[5kge]], [[5kgg]], [[5kgi]], [[5kgk]], [[5kzi]], [[5vua]], [[5vub]], [[5vuc]], [[6mt0]], [[6vrv]], [[7oov]], [[7oow]], [[7oox]], [[7xsv]] – hPim1 catalytic domain + inhibitor
**[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor
*Pim1 kinase domain residues 92-404
**[[4jx3]] – hPim1 kinase domain
**[[3uix]], [[5c1q]] – hPim1 kinase domain residues 120-404 + quinoline derivative
**[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate
**[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand
**[[1xws]], [[4alu]], [[4alv]], [[4alw]], [[4as0]], [[4bzn]], [[4bzo]], [[4dtk]], [[4jx7]], [[4rbl]], [[4rc2]], [[4rc3]], [[4rc4]], [[4ty1]], [[4wrs]], [[4wsy]], [[4wt6]], [[4xhk]], [[5dgz]], [[5dhj]], [[5dia]], [[5dwr]], [[5eol]], [[5kcx]], [[5o11]], [[5o12]], [[5o13]], [[5tel]], [[5tex]], [[5toe]], [[5v80]], [[5v82]]. [[6bsk]], [[6kzi]], [[6l11]], [[6l12]], [[6l13]], [[6l14]], [[6l15]], [[6l16]], [[6l17]], [[6no8]], [[6no9]], [[6vru]], [[6ykd]], [[7zun]] – hPim1 kinase domain + inhibitor
**[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor
*Pim1 full length
**[[4rpv]], [[5tur]] - hPim1 + inhibitor
*Pim1 complex with consensus peptide (pimtide)
**[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6qxk]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]] – hPim1 kinase domain + inhibitor + consensus peptide
**[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide
**[[2c3i]], [[5ndt]], [[5n5m]], [[5n5l]], [[5n52]], [[5n51]], [[5n50]], [[5n4z]], [[5n4y]], [[5n4x]], [[5n4v]], [[5n4u]], [[5n4r]], [[5n4o]], [[5n4n]], [[5mzl]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide
**[[4gw8]], [[7qb2]], [[7qfm]], [[7z6u]], [[8afr]] – hPim1 catalytic domain (mutant) + inhibitor + pimtide
**[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide
**[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide
*Pim1 containing phosphorylated Ser 261
**[[1yhs]] – hPim1 kinase domain + PSer + staurosporine
**[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor
**[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor
**[[1yi4]] – hPim1 kinase domain + PSer + adenosine
*Pim2
**[[4x7q]] – hPim2 catalytic domain + inhibitor
**[[2iwi]] – hPim2 catalytic domain + Ru ligand
*'''Rip or receptor-interacting Chk; Domains – catalytic 1-294; Amyloid fibril 418-518; Death 561-671'''
**[[6ac5]] – hRip1 death domain
**[[6r5f]], [[6nw2]], [[6c4d]], [[6c3e]], [[5tx5]], [[7fcz]], [[7fd0]], [[7ydx]] – hRip1 catalytic domain + inhibitor
**[[6rln]], [[6ocq]], [[6nyh]], [[6hho]] – hRip1 catalytic domain (mutant) + inhibitor
**[[6ggs]] – hRip2 – Cryo EM
**[[5yrn]] – hRip2 CARD domain 434-540 – Cryo EM
**[[6szj]], [[6sze]], [[6s1f]], [[6rna]], [[6rn8]], [[6hmx]], [[6fu5]], [[6es0]], [[5w5o]], [[5w5j]] – hRip2 catalytic domain + inhibitor
**[[6ul8]] – hRip2 catalytic domain (mutant) + inhibitor
**[[8aza]] – hRip2 catalytic domain + XiaP Bir2 domain – Cryo EM
**[[7mx3]] – hRip3 catalytic domain (mutant) + inhibitor
**[[7mon]] – hRip3 catalytic domain (mutant) + MLKL
**[[7dac]] – hRip3 amyloid fibril - NMR
**[[7da4]] – hRip3 amyloid fibril – Cryo EM
**[[6oko]] – mRip3 catalytic domain + inhibitor
**[[6jpd]] – mRip3 residues 409-486 - NMR
**[[5wnm]], [[5wnj]] – mRip4 catalytic domain (mutant) + drug
**[[5wnl]] – mRip4 catalytic domain (mutant) + staurosporine
**[[5wnk]] – mRip4 catalytic domain (mutant) + inhibitor
**[[5wni]] – mRip4 catalytic domain (mutant) + ATP
**[[6gwm]] – rRip2 caspase recruitment domain 433-539
*'''Ulk'''
**[[6qas]] – hChk Ulk1 + inhibitor
**[[5ci7]], [[6mnh]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[8soi]], [[8sqz]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein
**[[8srm]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein – Cryo EM
**[[8srq]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein + PI3K – Cryo EM
**[[6qav]], [[6qau]], [[6qat]], [[6yid]] – hChk Ulk2 + inhibitor
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[6fdz]], [[6fdy]] – hChk Ulk3 + leukemia drug
**[[6tsz]] – hChk Ulk4 pseudfokinase domain + ATPgS
**[[6u5l]] – hChk Ulk4 (mutant) + inhibitor
*'''Hipa''' and '''Hipb'''
**[[3tpd]], [[3tpe]] – EcChk Hipa – ''Escherichia coli''
**[[3tpb]], [[3dnt]], [[3dnu]] – EcChk Hipa (mutant)
**[[4pu7]], [[4pu8]] – SoChk Hipb - ''Shewanella oneidensis''
**[[3tpt]] – EcChk Hipa (mutant) + ADP
**[[3fbr]] – EcChk Hipa (mutant) + AMPPNP + peptide
**[[3tpv]] – EcChk Hipa + ADP
**[[2wiu]] – EcChk Hipa + Hipb
**[[4yg7]], [[5k98]], [[3hzi]], [[3dnv]] – EcChk Hipa + Hipb + DNA
**[[4yg1]], [[4z58]], [[4z59]], [[4z5c]], [[4z5d]] – EcChk Hipb + DNA
**[[4z5h]] – EcChk Hipb (mutant) + DNA
**[[4pu3]], [[4pu4]] – SoChk Hipa + Hipb + DNA - ''Shewanella oneidensis''
**[[4pu5]] – SoChk Hipa + AMPPNP
*'''Chk Smg'''
**[[6l53]] – hChk Smg1 – Cryo EM
**[[7pw6]] – hChk Smg1 + inhibitor – Cryo EM
**[[7pw7]] – hChk Smg1 + Smg9 + inhibitor – Cryo EM
**[[7pw9]] – hChk Smg1 + Smg9 + AMPPNP + ATP – Cryo EM
**[[6l54]], [[6syt]] – hChk Smg1 + Smg8 + Smg9 – Cryo EM
**[[7pw4]], [[7pw5]] – hChk Smg1 + Smg8 + Smg9 + inhibitor – Cryo EM
**[[7pw8]] – hChk Smg1 + Smg8 + Smg9 + AMPPNP – Cryo EM
**[[6z3r]] – hChk Smg1 + Smg8 + Smg9 + regulator of nonsense transcripts – Cryo EM
**[[2hwy]] – hChk Smg5 PIN domain
**[[2hww]], [[2hwx]] – hChk Smg6 PIN domain (mutant)
**[[4um2]] – hChk Smg6 TPR domain
**[[1ya0]] – hChk Smg7 N terminal
*'''Chk Vprbp or DCAF1'''
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain 1039-1401 (mutant)
**[[7sse]], [[7ufv]], [[8f8e]], [[8og5]], [[8og6]], [[8og7]], [[8og8]], [[8og9]], [[8oga]], [[8ogb]], [[8ogc]], [[8oo5]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) + inhibitor
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[5aja]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
*'''Other Chk'''
**[[1wak]] – hChk Sprk1
**[[3dak]] – hChk Osr1 kinase domain
**[[7okw]] – hChk Osr1 C-terminal
**[[4aw2]] – hChk Mrckα kinase domain
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain (mutant)
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM
**[[1uf0]] – hChk Dcamkl1 DCX domain – NMR
**[[1u5q]] – rChk Tao2 kinase domain
**[[2cos]] – mChk Lats2 – NMR
**[[1xte]], [[1xtn]], [[6edx]] – mChk Sgk3 PX domain
**[[4yom]] – mChk Brsk2
**[[4ynz]] – mChk Brsk1 N terminal domain
**[[5iri]] – mChk Brsk1 residues 592-719
**[[5oat]], [[7mp8]] – rfbChk Pink1– red flour beetle
**[[7t3x]] – Chk Pink1 (mutant) – louse
**[[4f0g]] – smChk Roco4 kinase domain – slime mold
**[[5tos]] – AtChk Bik1
**[[1q8z]], [[1zyc]] – yChk
**[[1how]], [[1zxe]], [[1zy4]] – yChk (mutant)
**[[1ow5]], [[1x9x]] – yChk Ste11 SAM domain – NMR
**[[2kio]], [[2kit]], [[1w1n]] – yChk Tor1 FATC domain – NMR
**[[3gre]] – yChk Vps15 WD repeat domain
**[[3osm]], [[3ost]] - yChk Kcc4 kinase domain
**[[5yyx]] – yChk Mek1 FHA domain
**[[6jxc]], [[6jxa]] – yChk Tel1 – Cryo EM
**[[6u69]] – CaChk Yck2 – ''Candida albicans''
**[[6sl1]], [[6sl0]], [[6skz]], [[6sky]] – Chk Tel1 – ''Chaetonium thermophilum'' – Cryo EM
**[[6ra0]] – CeChk Dkf1 – ''Chaenorhabditis elegans''
**[[7z6e]] – CeChk Mrck1 regulatory domain
**[[6tlb]] – Chk – ''Plasmodium falciparum''
*Other Chk complexes
**[[1wbp]], [[7dd1]] – hChk Sprk1 + peptide
**[[3beg]] – hChk Srpk1 + splicing factor SF2
**[[3hdm]], [[3hdn]], [[7pue]] – hChk Sgk1 (mutant) + inhibitor
**[[2r5t]] – hChk Sgk3 + AMPPNP
**[[4yff]], [[4yfi]], [[6b5j]], [[7mgj]], [[7mgk]] – hChk Tnni3k + inhibitor
**[[2v3s]] – hChk Osr1 + hChk Wnk4 peptide
**[[2vwi]] – hChk Osr1 kinase domain + ANP
**[[7que]], [[7quf]] – hChk Drak1 kinase domain + inhibitor
**[[4crs]] – hChk N2 kinase domain + ATPγS
**[[3tku]], [[4ual]], [[3qfv]], [[5ote]], [[5otf]] – hChk Mrckβ + inhibitor
**[[4uak]] – hChk Mrckβ + ADP
**[[5aja]], [[4z8l]], [[4cc9]] – hChk Vprbp WD repeat domain + VPX + SAMHD1
**[[5jk7]] – hChk Vprbp WD repeat domain + VPX + DDB1 + UDG
**[[3wa0]], [[4p7i]] – hChk Vprbp residues 1417-1506 + merlin
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor
**[[5ci7]] – hChk Ulk1 (mutant) + inhibitor
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog
**[[5b5w]], [[5b6b]], [[5brk]] – hChk Lats1 residues 622-704 + MOB1
**[[5yz0]] – hChk Atr + Atr-interacting protein – Cryo EM
**[[6bdn]] – hChk Tao3 kinase domain + ADP
**[[5yh3]] – hChk Fam20C 141-578 + pseudokinase Fam20A
**[[2gcd]] – rChk Tao2 kinase domain + staurosporine
**[[1u5r]] – rChk Tao2 kinase domain + ATP
**[[5yj9]], [[7mp9]] – rfbChk Pink1 kinase domain + AMPPNP
**[[6bn1]] – DmChk Hippo SARAH domain + Shar-Pei
**[[3hgk]] – Chk Pto + effector protein AVRPTOB – Currant tomato
**[[3p86]], [[3ppz]] - AtChk Ctr1 + staurosporine
**[[4f0f]] – smChk Roco4 kinase domain + APPCP
**[[4f1m]], [[4f1o]] – smChk Roco4 kinase domain (mutant) + APPCP
**[[4f1t]], [[4yzm]], [[4yzn]] – smChk Roco4 kinase domain + inhibitor
**[[5fvm]] - Tor2 + LST8 - ''Kluyveromyces marxianus''
**[[5kc2]] - yVps15 + Vps34 - Cryo EM
**[[5dfz]] - yVps15 + Vps34 + Vps30 + VPSAP28 + VPSAP30 - Cryo EM
**[[1q8y]], [[1q97]], [[1q99]], [[1zyd]] – yChk + nucleotide
**[[1zy5]] – yChk (mutant) + nucleotide
**[[2jd5]] – yChk + NPL-3P
**[[4lqs]], [[4lqq]], [[4lqp]] – yChk Cbk1 residues 251-756 + Cbk1 activator Mob2
**[[6emk]] – yChk Tor2 + LST8 + TSC11 + AVO1 + AVO2 – Cryo EM
**[[6s8f]] – yChk Tel1 + AMPPNP – Cryo EM
**[[5yyz]] – yChk Mek1 FHA domain + Hop1
**[[5x6o]], [[6z3a]], [[7wzr]], [[7wzw]]– yChk Mec1 + LCD1 – Cryo EM
**[[6z2w]], [[6z2x]] – yChk Mec1 (mutant) + LCD1 – Cryo EM
**[[7kue]] – yChk Kin28 in TFIIK complex – Cryo EM
**[[6u6a]] – CaChk Yck2 + inhibitor
**[[5fvm]] – Chk Tor2 + LST8 – ''Kluyveromyces maximanus''
*Serine/threonine protein kinase Rad53 see [[Rad53]]
*Serine/threonine protein kinase Gsk3B see [[Glycogen synthase kinase 3]]
}}
[[Category:Topic Page]]

Serine/threonine protein kinase 3D structures

2026-08-16T10:39:33Z

Michal Harel:

==3D structures of serine/threonine protein kinase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Chk1'''; domains - kinase 1-289; KA1 393-492

**[[1ia8]] – hChk1 kinase domain – human 
**[[5w12]] – hChk1 KA1 domain 
**[[1zlt]] – hChk1 kinase domain + hymenaldisine 
**[[1nvq]], [[1nvr]] – hChk1 kinase domain + peptide + saurosporine

**[[1nvs]], [[1zys]], [[7ako]] - hChk1 kinase domain + peptide + inhibitor
**[[7akm]] - hChk1 kinase domain + ATP 
**[[2cgu]], [[2cgv]], [[2cgw]], [[2cgx]], [[2c3j]], [[2c3k]], [[2c3l]], [[2br1]], [[2brb]], [[2brg]], [[2brh]], [[2brm]], [[2brn]], [[2bro]], [[2ayp]], [[2gdo]], [[2ghg]], [[2hog]], [[2ywp]], [[2hxl]], [[2hxq]], [[2hy0]], [[2r0u]], [[2e9n]], [[2e9o]], [[2e9p]], [[2e9u]], [[2e9v]], [[2qhm]], [[2qhn]], [[3f9n]], [[2wmq]], [[2wmr]], [[2wms]], [[2wmt]], [[2wmu]], [[2wmv]], [[2wmx]], [[3jvr]], [[3jvs]], [[2xey]], [[2xf0]], [[2xez]], [[2x8d]], [[2x8e]], [[2x8i]], [[3ot3]], [[3ot8]], [[3pa3]], [[3pa4]], [[3pa5]], [[3nlb]], [[2wmw]], [[2ydi]], [[2ydj]], [[2ydk]], [[2yer]], [[2yex]], [[2ym3]], [[2ym4]], [[2ym5]], [[2ym6]], [[2ym7]], [[2ym8]], [[3tkh]], [[3tki]], [[3u9n]], [[4fsm]], [[4fsn]], [[4fsq]], [[4fsr]], [[4fst]], [[4fsu]], [[4fsw]], [[4fsy]], [[4fsz]], [[4ft0]], [[4ft3]], [[4ft5]], [[4ft7]], [[4ft9]], [[4fta]], [[4ftc]], [[4fti]], [[4ftj]], [[4ftk]], [[4ftl]], [[4ftm]], [[4ftn]], [[4fto]], [[4ftq]], [[4ftr]], [[4ftt]], [[4ftu]], [[4gh2]], [[4hyh]], [[4hyi]], [[4jik]], [[4rvm]], [[4rvl]], [[4rvk]], [[4qyh]], [[4qyg]], [[4qyf]], [[4qye]], [[5dls]], [[5f4n]], [[6fc8]], [[5fcf]], [[5fck]], [[6fck]], [[6fcf]], [[7bko]], [[8e80]], [[8e81]] - hChk1 kinase domain + inhibitor 
**[[5oot]], [[5op2]], [[5op4]], [[5op5]], [[5op7]], [[5opb]], [[5opr]], [[5ops]], [[5opu]], [[5opv]], [[5oq5]], [[5oq6]], [[5oq7]], [[5oq8]], [[7bjd]], [[7bjh]], [[7bjj]], [[7bjm]], [[7bjo]], [[7bjr]], [[7bjx]], [[7bk1]], [[7bk2]], [[7bk3]], [[7mck]], [[7suf]], [[7sug]], [[7suh]], [[7sui]], [[7suj]], [[8siv]], [[8siw]], [[8six]] - hChk1 kinase domain (mutant) + inhibitor 
**[[5oop]] - hChk1 kinase domain (mutant) + AMPPNP 
**[[5oor]] - hChk1 kinase domain (mutant) + staurosporine 
**[[7bkn]] - hChk1 kinase domain + adenine 
**[[7bje]] - hChk1 kinase domain (mutant) + adenine 
**[[2jqi]] – yChk1 – yeast 

*'''Chk2 (Checkpoint kinase)'''

**[[1gxc]] – hChk2 phosphothreonine-binding domain + phosphopeptide

**[[2cn5]] – hChk2 kinase domain + ADP

**[[2cn8]] – hChk2 kinase domain + inhibitor

**[[2w0j]], [[2w7x]], [[2wtc]], [[2wtd]], [[2xbj]], [[2xm8]], [[2xm9]], [[2yiq]], [[2yir]], [[2yit]], [[2cn8]], [[2ycf]], [[2ycq]], [[2ycr]], [[2ycs]], [[2wti]], [[2wtj]], [[2xk9]], [[4a9r]], [[4a9s]], [[4a9t]], [[4bda]], [[4bdb]], [[4bdc]], [[4bdd]], [[4bde]], [[4bdf]], [[4bdg]], [[4bdh]], [[4bdi]], [[4bdj]], [[4bdk]], [[2uv2]] - hChk2 kinase domain + inhibitor

**[[3i6u]], [[3i6w]] – hChk2 residues 84-502 (mutant)

*'''Chk3 (Mst2)'''; domains - kinase 13-313; SARAH 436-484

**[[4hkd]], [[4l0n]], [[4oh9]], [[3wws]] – hChk3 SARAH domain 
**[[4lg4]] – hChk3 kinase domain 
**[[4lgd]] – hChk3 kinase domain + RASSF5 SARAH domain 
**[[6ao5]] – hChk3 kinase+SARAH domains (mutant) + SAV1 SARAH domain 
**[[5dh3]], [[8a66]] – hChk3 kinase domain + inhibitor 

*'''Chk4 (Mst1)''' ; Domains – kinase 1-311; SARAH 432-480

**[[3com]] – hChk4 kinase domain 
**[[6yat]], [[8a5j]]– hChk4 kinase domain + inhibitor 
**[[4nr2]] – hChk4 SARAH domain 
**[[2jo8]] – hChk4 SARAH domain - NMR 
**[[4oh8]] – hChk4 SARAH domain + Ras association domain-containing protein 

*'''Chk5 (Aurora kinase b)'''

**[[4af3]] – hChk5 + inhibitor 

*'''Chk6 or Chk15 or Aurora kinase A'''

**[[1muo]], [[1mq4]], [[4j8n]], [[6cpe]], [[4o0s]] – hChk6 kinase domain 
**[[4bn1]], [[4o0w]], [[4o0u]] – hChk6 kinase domain (mutant) 
**[[5dnr]], [[5drd]], [[5dt3]] – hChk6 kinase domain + ATP 
**[[5drd]] – hChk6 kinase domain + ATP 
**[[1ol6]] – hChk6 kinase domain (mutant) + ATP 
**[[2wqe]] – hChk6 kinase domain (mutant) + ADP 
**[[5odt]] – hChk6 kinase domain (mutant) + ADP + TACC3 
**[[2c6d]] – hChk6 kinase domain (mutant) + ADPNP 
**[[2dwb]] – hChk6 kinase domain + AMPPNP 
**[[6cpf]] – hChk6 kinase domain + AMPPCP 
**[[5g15]] – hChk6 kinase domain + AMPPNP + monobody 
**[[6cpg]], [[8ssp]] – hChk6 kinase domain + inhibitor + monobody 
**[[2j4z]], [[2j50]], [[2np8]], [[3efw]], [[2x81]], [[2x6d]], [[2x6e]], [[3myg]], [[3vap]], [[4b0g]], [[4j8m]], [[5dpv]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5one]], [[5obr]], [[4byi]], [[4byj]], [[4jai]], [[4jaj]], [[3w10]], [[3w16]], [[3w18]], [[3w2c]], [[4uzh]], [[4uzd]], [[4uyn]], [[4zs0]], [[4ztq]], [[4ztr]], [[4zts]], [[5aad]], [[5aae]], [[5aag]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5obr]], [[5one]], [[6gra]], [[6c2t]], [[6c2r]], [[5zan]], [[6z4y]], [[7ayh]], [[7ayi]], [[7fic]], [[7o2v]], [[8jmx]] – hChk6 kinase domain + inhibitor 
**[[2bmc]], [[2c6e]], [[3coh]], [[3h0y]], [[3h0z]], [[3h10]], [[3fdn]], [[2wtw]], [[3lau]], [[3nrm]], [[2xne]], [[2xng]], [[2xru]], [[3k5u]], [[3m11]], [[3p9j]], [[3r21]], [[3r22]], [[3qbn]], [[3unz]], [[3uo4]], [[3uo5]], [[3uo6]], [[3uod]], [[3uoh]], [[3uoj]], [[3uok]], [[3uol]], [[3up2]], [[3up7]], [[4dhf]], [[4dea]], [[4deb]], [[4ded]], [[4dee]], [[5aad]], [[5aae]], [[5aaf]], [[5aag]], [[4jbo]], [[4jbp]], [[4jbq]], [[4prj]], [[5dpv]], [[6hjk]], [[6hjj]] – hChk6 kinase domain (mutant) + inhibitor 
**[[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor 
**[[5dos]], [[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor 
**[[5dn3]], [[5dos]], [[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor 
**[[6c83]] – hChk6 kinase domain + AMPPCP + nanobody 
**[[8sso]] – hChk6 kinase domain + drug + monobody 
**[[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor 
**[[5g1x]], [[7ztl]] – hChk6 kinase domain (mutant) + N-Myc 
**[[8guw]] – hChk6 kinase domain/activator peptide 
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + new antigen receptor variable domain 
**[[5lxm]] – hChk6 kinase domain (mutant) + Targeting protein for XKLP2 
**[[3daj]], [[3d14]], [[3dj5]], [[3dj6]], [[3dj7]], [[3d15]], [[3d2i]], [[3d2k]] – Chk6 kinase domain (mutant) + inhibitor - mouse 

*Chk6 with phosphorylated Thr 287, Thr288

**[[1ol5]], [[1ol7]] – hChk6 kinase domain + PThr + ADP 
**[[5dnr]], [[5dt3]] – hChk6 kinase domain + PThr + ATP 
**[[2w1c]], [[2w1d]], [[2w1e]], [[2w1f]], [[2w1g]], [[5dn3]] – hChk6 kinase domain + PThr + inhibitor 
**[[2wtv]], [[5orl]], [[5orn]], [[5oro]], [[5orp]], [[5orr]], [[5ors]], [[5ort]], [[5orv]], [[5orw]], [[5orx]], [[5ory]], [[5orz]], [[5os0]], [[5os1]], [[5os2]], [[5os3]], [[5os4]], [[5os5]], [[5os6]], [[5osd]], [[5ose]], [[5osf]] – hChk6 kinase domain (mutant) + PThr + inhibitor 
**[[3e5a]], [[3ha6]] – hChk6 kinase domain + PThr + inhibitor + targeting protein for XKLP2 
**[[5g1x]] – hChk6 kinase domain (mutant) + PThr + N-Myc 
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + PThr + new antigen receptor variable domain 
**[[5lxm]] – hChk6 kinase domain (mutant) + PThr + TPX2 
**[[6r4d]], [[6r4c]], [[6r4b]], [[6r4a]] – hChk6 kinase domain + PThr + inhibitor + ADP 
**[[6i2u]] – hChk6 kinase domain (mutant) + PThr + inhibitor + ADP 
**[[6r49]] – hChk6 kinase domain (mutant) + PThr + CoA 

*'''Chk10 (lymphocyte-oriented kinase)''' or LOK or STK10

**[[7qgp]] – hChk10 
**[[2j7t]], [[4aot]], [[4equ]], [[4usd]], [[4use]], [[5ajq]], [[5owq]], [[5owr]], [[6eim]], [[6gtt]], [[6i2y]], [[6hxf]] – hChk10 kinase domain + inhibitor 
**[[4bc6]], [[6i2y]] – hChk10 + drug 

*'''Chk11'''

**[[2wtk]] – hChk11 (mutant) + calcium-binding protein 

*'''Chk12-A (Aurora kinase b-a or Aurora B kinase)'''

**[[2vgo]], [[2vgp]], [[2vrx]], [[3ztx]], [[4c2v]], [[5eyk]] – fChk12-A + inner centromere protein A peptide + inhibitor - frog 
**[[4c2w]] – fChk12-A + inner centromere protein A peptide + AMPPNP 
**[[4b8l]], [[4b8m]], [[5k3y]] – fChk12-A (mutant) + inner centromere protein A peptide + inhibitor 

*'''Chk13 (Polo-like kinase Plk)'''

*Plk1 Polo-box domain (Pbd) 371-594''

**[[1q4o]], [[2ogq]], [[3hih]], [[3p2w]], [[4h5x]], [[6n46]] – hPlk1 Pbd 

*Plk1 Pbd complex with polypeptide

**[[1umw]], [[2ojx]], [[3bzi]], [[3c5l]], [[3rq7]], [[4dfw]], [[4whl]], [[4whk]], [[4whh]], [[4rcp]], [[4o6w]], [[4o56]], [[5dms]], [[5dmv]], [[5dnj]] , [[7mso]], [[7mx1]] – hPlk1 + peptide 
**[[3hik]], [[3fvh]], [[3p2z]], [[3p34]], [[3p35]], [[3p36]], [[3p37]], [[3q1i]], [[4e67]], [[4e9c]], [[4e9d]], [[4hab]], [[4hy2]], [[4o9w]], [[4x9r]], [[4x9v]], [[4x9w]], [[5j19]], [[6gy2]] – hPlk1 + phosphopeptide 
**[[1q4k]] – hPlk1 (mutant) + phosphopeptide 
**[[2v5q]] – hPlk1 + design ankyrin repeat protein 
**[[4lkl]] – hChk Plk1 + PL-55 
**[[4lkm]] – hChk Plk1 + PL-74 
**[[6ax4]] – hChk Plk1 + histidine cyclized macrocycle 
**[[5x3s]] – mPlk1 + phosphopeptide 
**[[8joq]], [[8joy]] – hPlk1 Pbd + hpv peptide 

*Plk1 Pbd complex with small molecule inhibitor

**[[4h71]], [[4hco]], [[5ta6]], [[5ta8]], [[8bjt]], [[8crc]] – hPlk1 + inhibitor 
**[[2rku]] – hPlk1 (mutant) + inhibitor 
**[[3db6]], [[3db8]], [[3dbc]], [[3dbd]], [[3dbe]], [[3dbf]] – zfPlk1 (mutant) + inhibitor – zebra fish 

*Plk1 catalytic domain 36-345

**[[2owb]] – hPlk1 catalytic domain (mutant) 
**[[2ou7]] – hPlk1 catalytic domain (mutant) + AM
**[[3kb7]], [[2yac]], [[3thb]], [[4a4l]], [[4a4o]] – hPlk1 catalytic domain + inhibitor 
**[[3fc2]] – hPlk1 catalytic domain (mutant) + inhibitor 
**[[4j52]], [[4j53]] – hChk Plk1 (mutant) + inhibitor 
**[[3d5x]] – zfPlk1 catalytic domain (mutant) + wortmannin 
**[[3d5w]] – zfPlk1 catalytic domain + ADP 

*'''Plk2'''

**[[4i5m]], [[4i5p]], [[4i6b]], [[4i6f]], [[4i6h]] – hChk Plk2 kinase domain (mutant) + inhibitor 
**[[4xb0]], [[4rs6]] – hChk Plk2 Pbd 

*'''Plk3'''

**[[4b6l]], [[4i6b]] – hChk Plk3 kinase domain + inhibitor 

*'''Plk4'''; Domains – kinase 2-275; Pbd 580-808; Pb3 884-970

**[[3cok]] – hChk Plk4 kinase domain 
**[[4n9j]] – hChk Plk4 Pbd domain 
**[[4n7z]], [[4n7v]] – hChk Plk4 Pbd domain + centrosomal protein 
**[[6w38]], [[6w3i]] – hChk Plk4 Pbd domain + Fam46C 
**[[6w3j]] – hChk Plk4 Pbd domain + Fam46C + CEP92 peptide 
**[[4jxf]], [[4yur]] – hChk Plk4 kinase domain + inhibitor 
**[[5lhy]] – hChk Plk4 Pb3 domain 
**[[4yyp]], [[5lhz]] – hChk Plk4 Pb3 domain + Scl-interrupting locus protein 
**[[4nk7]], [[4g7n]], [[5lhx]], [[7rl3]] – DmChk Plk4 Pbd domain – ''Drosophila melanogaster'' 

*'''Chk16'''

**[[2buj]] – hChk16 (mutant) + staurosporin 

*'''Chk17B''' or DRAK2 or STK17B

**[[3lm0]] – hChk17B 
**[[6qf4]], [[7q7c]], [[7q7d]] – hChk17B + ADP 
**[[7q7e]] – hChk17B + ATP 
**[[3lm5]] – hChk17B + quercetin 
**[[6y6f]], [[6y6h]], [[6zjf]] – hChk17B + pyrimidine derivative 
**[[7akg]] – hChk17B + drug 

*'''Chk19''' or STK19

**[[7xrb]] – hChk19 

*'''Chk24 (Mst3)''' or STK24

**[[3a7f]], [[3a7g]], [[3a7h]], [[3a7i]], [[3a7j]], [[3ckw]] – hChk24 kinase domain 
**[[4w8e]], [[4w8d]], [[4u8z]], [[4qmm]], [[4qmn]], [[4qmo]], [[4qmp]], [[4qmq]], [[4qms]], [[4qmt]], [[4qmu]], [[4qmv]], [[4qmw]], [[4qmx]], [[4qmy]], [[4qmz]], [[4qna]], [[4qo9]], [[4u8z]], [[7b30]], [[7b31]], [[7b32]], [[7b33]], [[7b34]], [[7b35]], [[8bzi]], [[8bzj]], [[8qlr]], [[8qls]], [[8qlt]] – hChk Mst3 + inhibitor 
**[[8qlq]] – hChk Mst3 + macrocyclic inhibitor 
**[[3ckx]] – hChk24 kinase domain + staurosporin 
**[[3zhp]] – hChk24 kinase domain + calcium-binding protein 
**[[4o27]] – hChk24 kinase domain (mutant) + calcium-binding protein 
**[[4qml]] – hChk Mst3 kinase domain + AMPPNP 

*'''Chk25 or STK25'''

**[[2xik]] – hChk25 kinase domain 
**[[7z4v]] – hChk25 kinase domain + inhibitor 
**[[3w8h]] – hChk25 regulatory domain + programmed cell death protein 10 
**[[4nzw]] – hChk25 kinase domain (mutant) + calcium-binding protein 

*'''Chk26 (Mst4)'''

**[[3ggf]], [[7b36]] – hChk Mst4 + inhibitor 
**[[4geh]], [[3w8i]] - hChk Mst4 dimerization domain + programmed cell death protein 10 
**[[4fza]], [[4fzd]], [[4fzf]] – hChk Mst4 (mutant) + calcium-binding protein 

*'''Chk32'''

**[[4fr4]] – hChk32A 

*'''Chk38'''

**[[6bxi]] – hChk38 kinase domain 

*'''Chk39''' or SPAK

**[[7o86]] – hChk39 C-terminal 
**[[5d9h]] – mChk39 residues 63-403 + ATP 
**[[5dbx]] – mChk39 residues 63-403 (mutant) + AMPPNP 

*'''Chk40'''

**[[5l2q]] – hChk40 kinase homology domain 

*'''Dclk1'''

**[[6kyq]] – hChk Dclk1 kinase domain 
**[[6kyr]] – hChk Dclk1 kinase domain (mutant) 
**[[5jzj]] – hChk Dclk1 kinase domain + AMPPN 
**[[5jzn]], [[7kx6]], [[7kxw]] – hChk Dclk1 kinase domain + inhibitor 
**[[7f3g]] – hChk Dclk1 kinase domain + drug 
**[[7kx8]] – hChk Dclk1 C-terminal + inhibitor 

*'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123; kinase 144-480

**[[1unp]], [[1unr]] – hRac-α hChk pleckstrin homology domain 
**[[2uzr]], [[2uzs]], [[7myx]] – hRac-α hChk pleckstrin homology domain (mutant) 
**[[1h10]], [[1unq]], [[2uvm]] – hRac-α hChk pleckstrin homology domain + inositol tetrakisphosphate 
**[[3o96]], [[4ejn]], [[6s9w]], [[6s9x]], [[6hhj]], [[6hhi]], [[6hhh]], [[6hhg]], [[6hhf]] - hRac-α hChk + inhibitor 
**[[5kcv]], [[7nh4]], [[7nh5]] - hRac-α hChk (mutant) + inhibitor 
**[[4gv1]], [[4ekl]] - hRac-α hChk kinase domain + inhibitor 
**[[3qkm]], [[6ccy]] - hRac-α hChk kinase domain (mutant) + inhibitor 
**[[6buu]] - hRac-α hChk kinase domain + bisubstrate peptide 
**[[4ekk]] - hRac-α hChk kinase domain (mutant) + GSK3 peptide + AMPPNP 
**[[6npz]] - hRac-α hChk kinase domain + peptide + inhibitor 
**[[3ow4]], [[3qkk]], [[3qkl]], [[6buu]] - hRac-α hChk kinase domain (mutant) + peptide + inhibitor 
**[[7apj]] - hRac-α hChk + nanobody 

*'''Rac-β hChk (AKT2)'''

**[[1gzk]], [[1gzn]], [[1gzo]], [[1mrv]], [[1mry]] – hRac-β hChk kinase domain 
**[[1p6s]] - hRac-β hChk pleckstrin homology domain - NMR 
**[[1o6k]] - hRac-β hChk kinase domain + GSK3 peptide + AMPPNP 
**[[2jdo]], [[2jdr]], [[2uw9]], [[2x39]], [[3cqu]], [[3cqw]] - hRac-β hChk kinase domain + GSK3 peptide + inhibitor 
**[[3e87]], [[3e88]], [[3e8d]] - Rac-β hChk kinase domain (mutant) + GSK3 peptide + inhibitor 
**[[3d0e]], [[8q61]] - hRac-β hChk kinase domain (mutant) + inhibitor 

*'''Rac-γ hChk (ATK3)'''

**[[2x18]] – Rac-γ hChk PH domain 

*'''A-Raf'''

**[[1wxm]] – hA-Raf RAS-binding domain 19-91 - NMR 
**[[2mse]] – hA-Raf RAS-binding domain + APOA-I + K-ras - NMR 

*'''B-Raf'''; domains - BRS 38-116; Ras-binding 153-237; kinase 445-723

**[[8dgs]], [[8dgt]] – hB-Raf in Ras/Raf complex – Cryo EM 
**[[7z37]], [[7z38]], [[7zr5]] – hB-Raf + Hsp90 + CDC37 + PP5 – Cryo EM 
**[[1uwh]], [[3c4c]], [[6v2u]], [[6xfp]], [[6xlo]], [[8f7o]], [[8f7p]] – hB-Raf kinase domain + anticancer drug 
**[[1uwj]], [[6p3d]] – hB-Raf kinase domain (mutant) + anticancer drug 
**[[2fb8]], [[3d4q]], [[3ii5]], [[3psd]], [[3skc]], [[3tv6]], [[4g9c]], [[4ksp]], [[4ksq]], [[3psb]], [[3ppj]], [[3ppk]], [[3prf]], [[3pri]], [[3tv4]], [[4dbn]], [[4e4x]], [[4mbj]], [[4ehe]], [[3q4c]], [[3q96]], [[3e26]], [[4h58]], [[4e26]], [[4fc0]], [[4pp7]], [[6cad]], [[7shv]] – hB-Raf kinase domain + pyrazole inhibitor 
**[[4jvg]], [[4ehg]], [[4fk3]], [[3idp]], [[4g9r]], [[4wo5]], [[4mnf]], [[4r5y]], [[4rzv]], [[4rzw]], [[4xv1]], [[4xv2]], [[4xv3]], [[4xv9]], [[4yht]], [[5c9c]], [[5hi2]], [[5ita]], [[5jrq]], [[5jsm]], [[5jt2]], [[6nsq]], [[6p7d]], [[6uuo]] – hB-Raf kinase domain (mutant) + pyrazole inhibitor 
**[[5csw]], [[5csx]], [[5ct7]], [[5fd2]], [[5hid]], [[5hie]], [[5val]], [[5vam]], [[6b8u]], [[6n0q]], [[6n0p]], [[7k0v]], [[7p3b]], [[7p3v]], [[8c7x]], [[8c7y]] - hB-Raf kinase domain + inhibitor 
**[[6v34]] – hB-Raf kinase domain (mutant) + inhibitor 
**[[4mne]] – hB-Raf kinase domain + MAPKK1 
**[[8f7o]] – hB-Raf kinase domain + drug 
**[[7m0u]] – hB-Raf kinase domain + AMPPNP + drug 
**[[6u2h]] – hB-Raf kinase domain + 14-3-3 ζ/δ 
**[[7mfe]] – hB-Raf + 14-3-3 ζ/δ – Cryo EM 
**[[7mff]] – hB-Raf + 14-3-3 ζ/δ + inhibitor – Cryo EM 
**[[7mfd]] – hB-Raf + 14-3-3 ζ/δ + MEK + inhibitor – Cryo EM 
**[[6pp9]] – hB-Raf kinase domain + MEK1 + ANP 
**[[7m0x]], [[7m0z]] – hB-Raf kinase domain + MEK1 + ANP + inhibitor 
**[[7m0t]], [[7m0u]], [[7m0v]], [[7m0w]], [[7m0y]] – hB-Raf kinase domain + MEK1 + ANP + drug 
**[[6u2g]] – hB-Raf kinase domain + MEK1 + AMPPCP 
**[[5vr3]] – hB-Raf BRS domain 
**[[7jhp]] – hB-Raf BRS domain + Hras 
**[[6ntc]], [[6ntd]] – hB-Raf BRS domain (mutant) + Hras 
**[[6xi7]] – hB-Raf 52-188 + Kras 
**[[2l05]], [[5j17]], [[5j2r]] – hB-Raf RAS-binding domain - NMR 
**[[3ny5]] – hB-Raf RAS-binding domain 
**[[5j18]] – hB-Raf RAS-binding domain + inhibitor - NMR 
**[[6pts]], [[6ptw]] – hB-Raf 56-187 + Kras + apolipoprotein + GMPPNP - NMR 
**[[6uan]], [[6q0k]] – hB-Raf + 14-3-3 ζ – Cryo EM 
**[[6nyb]] – hB-Raf + 14-3-3 ζ + MEK1 – Cryo EM 
**[[6q0t]], [[6q0j]] – hB-Raf (mutant) + 14-3-3 ζ + MEK1 – Cryo EM 

*'''c-Raf'''; Domains – RAS-binding (RBD) 55-132; Cys-rich 136-187 (CBD); kinase 323-618

**[[1rfa]], [[8jna]], [[8jof]], [[8jog]] – hc-Raf RBD - NMR 
**[[1faq]], [[1far]] – hc-Raf cysteine-rich domain - NMR 
**[[3omv]] – hc-Raf kinase domain 
**[[1rrb]] – c-Raf RBD – NMR - rat 

*c-Raf complex with protein

**[[8cpd]] – hc-Raf + 14-3-3 protein zeta – Cryo EM 
**[[9mmp]] – hc-Raf + MEK1 + 14-3-3 protein zeta – Cryo EM 
**[[9mmr]] – hc-Raf (mutant) + MEK1 + 14-3-3 protein zeta – Cryo EM 
**[[1c1y]] – hc-Raf RBD + RAP1A 
**[[3kuc]] – hc-Raf RBD (mutant) + RAP1A 
**[[1gua]] – hc-Raf RBD + RAP1A + GPPNHP 
**[[8jnb]] – hc-Raf RBD + ligand 
**[[4g0n]], [[4g3x]] – hc-Raf RBD + GTPase Hras 
**[[3kud]] – hc-Raf RBD (mutant) + GTPase Hras 
**[[8epw]], [[8t74]] – hc-Raf RBD + GTPase K-ras 
**[[8t75]], [[9ygs]] – hc-Raf RBD-CRD + GTPase K-ras + GMPPNP 
**[[9ay7]], [[9aya]] – hc-Raf + MEK1 
**[[9mmq]] – hc-Raf + MEK1 – Cryo EM 
**[[9mms]] – hc-Raf (mutant) + MEK1 – Cryo EM 
**[[9o0u]], [[9o0v]] – hc-Raf (mutant) + MEK1 + ANP + inhibitor– Cryo EM 
**[[8u1l]] – hc-Raf + Hsp90 + CDC37 – Cryo EM 
**[[8gae]], [[8gft]] – hc-Raf + Hsp90 + CDC37 + PP5 – Cryo EM 

*'''Snf1-related Chk'''

**[[3uc4]], [[3uc3]], [[3udb]], [[3zut]], [[3zuu]] – AtChk Srk2E kinase domain (mutant) – ''Arabidopsis thaliana'' 
**[[3ujg]] – AtChk Srk2E kinase domain (mutant) + protein phosphatase 2C 
**[[5yks]] – hChk 

*'''MAPK-interacting Chk''' or Mnk1 Mnk2

**[[2hw6]] – hMnk 1 catalytic domain 
**[[2hw7]] – hMnk 1 catalytic domain + staurosporin 
**[[5wvd]] – hMnk 1 catalytic domain + inhibitor 
**[[2ac3]] – hMnk 2 catalytic domain 
**[[2ac5]] – hMnk 2 catalytic domain (mutant) 
**[[6cj5]], [[6cje]], [[6cjh]], [[6cjw]], [[6cjy]], [[6ck3]], [[6ck6]], [[6cki]] – hMnk 2 catalytic domain (mutant) + inhibitor 

*'''hChk Pak''' or '''Chk N''' or '''PRK1'''; Domains - CRIB 74-109; Hr1B 122-199; catalytic 109-426; kinase 605-942

**[[1urf]] – hChk Pak-1 Hr1b domain - NMR 
**[[4nkg]] – hChk Pak-1 Hr1b domain + SSPH1 LRR domain 
**[[2rmk]] – hChk Pak-1 Hr1bb domain + Rac1 - NMR 
**[[1f3m]] – hChk Pak-1 autoregulatory+kinase domains 
**[[4otd]] - hChk Pak-1 kinase domain 
**[[1yhv]], [[1yhw]], [[3q4z]], [[3q52]], [[3q53]] – hChk Pak-1 kinase domain (mutant) 
**[[4o0r]], [[4o0t]], [[4zji]], [[4zjj]], [[4zlo]], [[4zy4]], [[4zy5]], [[4zy7]], [[5ime]], [[5kbq]], [[5kbr]], [[6b16]], [[7vto]] – hChk Pak-1 kinase domain + inhibitor 
**[[4oti]], [[4oth]], [[4otg]] – hChk Pak-1 kinase domain + inhibitor 
**[[4eqc]], [[4p90]], [[5dew]], [[5dey]], [[5dfp]] – hChk Pak-1 kinase domain (mutant) + inhibitor 
**[[2hy8]] – hChk Pak-1 kinase domain + staurosporin 
**[[2qme]] – hChk Pak-1 CRIB domain + RAC3 
**[[3fxz]], [[3fy0]], [[4daw]] – hChk Pak-1 kinase domain (mutant) + Ru complex 
**[[6fd3]] – hChk Pak-3 kinase domain (mutant) 
**[[2j0i]], [[4fie]] – hChk Pak-4 
**[[4fig]], [[4fij]], [[4l67]] – hChk Pak-4 kinase domain 
**[[2cdz]] – hChk Pak-4 + purine derivative 
**[[2ov2]] – hChk Pak-4 CRIB domain + RAC3 
**[[2qon]], [[4fif]], [[4fih]], [[4fii]], [[4jdh]], [[4jdi]], [[4jdj]], [[4jdk]], [[6wlx]], [[6wly]] – hChk Pak-4 kinase domain + peptide 
**[[4app]], [[4o0v]], [[4o0x]], [[4o0y]], [[4njd]], [[4xbu]], [[5bms]], [[5i0b]], [[5vee]], [[5vef]], [[5zjw]], [[5xvg]], [[5xvf]], [[5xva]], [[7cmb]], [[7cp3]], [[7cp4]] – hChk Pak-4 kinase domain + inhibitor 
**[[2x4z]], [[2xh5]] – hChk Pak-4 kinase domain (mutant) + inhibitor 
**[[5upl]], [[5upk]] – hChk Pak-4 kinase domain (mutant) + CDC42 
**[[5ved]] – hChk Pak-4 kinase domain + staurosporine 
**[[8ahi]] – hChk Pak-4 300-591 + inhibitor 
**[[7s46]], [[7s48]] – hChk Pak-4 catalytic domain + integrin beta-5 peptide 
**[[2c30]] – hChk Pak-6 
**[[2odb]] – hChk Pak-6 CRIB domain + CDC42 
**[[4ks8]] – hChk Pak-6 kinase domain + sunitinib 
**[[4ks7]] – hChk Pak-6 kinase domain (mutant) + inhibitor 
**[[2f57]] – hChk Pak-7 

*'''Mycobacterium tuberculosis Chk Pkn'''

**[[4x3f]] - MtChk PknA – ''Mycobacterium tuberculosis'' 
**[[4ow8]] - MtChk PknA kinase domain 
**[[3ori]], [[3ork]], [[3orl]], [[3orm]], [[3oro]], [[3orp]], [[3ort]] - MtChk PknB kinase domain (mutant) 
**[[1o6y]] – MtChk PknB kinase domain 
**[[6b2p]], [[6b2q]] – MtChk PknB kinase domain + inhibitor 
**[[2kud]], [[2kue]], [[2kuf]], [[2kui]] – MtChk PknB pasta domains 2-3 - NMR 
**[[3ouv]] – MtChk PknB pasta domain 3 
**[[5e0y]] – MtChk PknB pasta domain 4 
**[[5e10]] – MtChk PknB pasta domains 1-2 
**[[5e0z]] – MtChk PknB pasta domains 3-4 
**[[5e12]] – MtChk PknB pasta domains 2-4 
**[[5u94]] - MtChk PknB kinase domain + inhibitor 
**[[3f61]], [[3f69]] - MtChk PknB kinase domain (mutant) + inhibitor 
**[[6i2p]] - MtChk PknB kinase domain (mutant) + GARA + peptide 
**[[1rwi]], [[1rwl]] - MtChk PknD extracellular domain 
**[[2h34]] – MtChk PknE catalytic domain 
**[[7naa]] – MtChk PknF kinase domain + inhibitor 
**[[4y12]] - MtChk PknG + ATP-gS 
**[[4y0x]] - MtChk PknG + ADP 
**[[7q52]] - MtChk PknG + inhibitor 
**[[4esq]] - MtChk PknH extracellular domain 
**[[5m06]], [[5xka]] - MtChk PknI kinase domain 
**[[5m07]], [[5m08]], [[5m09]] - MtChk PknI kinase domain (mutant) 
**[[5xlm]], [[5xll]] - MtChk PknI sensor domain 
**[[7mxb]], [[7mxj]], [[7mxk]] - Chk PknG kinase domain + AMPPNP - Corynebacterium glutamicum 

*'''hChk Nek'''

**[[4apc]] – hChk Nek1 kinase domain (mutant) 
**[[4b9d]] - hChk Nek1 kinase domain (mutant) + inhibitor 
**[[2w5h]] – hChk Nek2 kinase domain 
**[[2jav]], [[2wqo]], [[2xk3]], [[2xk4]], [[2xk6]], [[2xk7]], [[2xk8]], [[2xkc]], [[2xkd]], [[2xke]], [[2xkf]], [[2xnm]], [[2xnn]], [[2xno]], [[2xnp]], [[4a4x]], [[4afe]], [[5m51]], [[5m53]], [[5m55]], [[5m57]], [[6sgd]], [[6sgh]], [[6sgi]], [[6sgk]], [[6sk9]] – hChk Nek2 + inhibitor 
**[[2w5a]], [[2w5b]] – hChk Nek2 + nucleotide 
**[[6tm5]] - hChk Nek2 in anaphase-promoting complex – Cryo EM 
**[[2wqm]], [[6s76]] – hChk Nek7 
**[[2wqn]] – hChk Nek7 + ADP 
**[[5de2]] – hChk Nek7 + hChk Nek9 
**[[6s73]], [[2wqo]] – hChk Nek7 + inhibitor 
**[[6npy]] – hChk Nek7 + Nlrp3 
**[[6s75]] – hChk Nek7 + inhibitor 

*'''Chk Rio'''

**[[6fdo]], [[6fdn]], [[6fdm]] – hChk Rio2 
**[[4otp]] – hChk Rio1 Rio domain + ADP 
**[[6hk6]], [[7vbt]] – hChk Rio2 + inhibitor 
**[[6eml]], [[6fai]], [[6g18]], [[6g51]], [[6rbd]],[[6rbe]], [[6y7c]] – yChk Rio2 in 40S particle – Cryo EM 
**[[1ztf]] – AfChk Rio1 + adenine derivative – Archaeoglobus fulgidus 
**[[1zth]] – AfChk Rio1 + ADP 
**[[1zp9]] – AfChk Rio1 + ATP 
**[[1tqp]], [[1zao]] – AfChk Rio2 + ATP 
**[[1zar]] – AfChk Rio2 + ADP 
**[[4gyg]] – CtChk Rio2 – Chaetonium thermophilum 
**[[4gyi]] – CtChk Rio2 + ADP 

*hChk Vrk (vaccinia-related kinase)

**[[2kty]], [[2kul]], [[2lav]], [[2rsv]] – hChk Vrk1 kinase domain 1-396 - NMR 
**[[3op5]] – hChk Vrk1 kinase domain (mutant) 
**[[5ukf]] – hChk Vrk1 kinase domain + inhibitor 
**[[5uvf]], [[6cnx]], [[6bu6]], [[6cfm]], [[6dd4]], [[6bp0]], [[6bru]], [[6btw]], [[6cmm]], [[6cqh]], [[6csw]], [[6npn]], [[6vxu]], [[6vzh]] – hChk Vrk1 kinase domain (mutant) + inhibitor 
**[[6ac9]] – hChk Vrk1 kinase domain (mutant) + AMPPNP 
**[[7tan]] – hChk Vrk1 kinase domain + nucleosome – Cryo EM 
**[[2v62]] – hChk Vrk2 kinase domain 
**[[5uu1]], [[6ncg]], [[8q1z]] – hChk Vrk2 kinase domain + inhibitor 

*Chk Wnk (protein kinase lysine-deficient); Domains - kinase 194-483; CCT1 454-549

**[[6cn9]], [[4q2a]], [[4pwn]] - hChk Wnk1 kinase domain (mutant) 
**[[5tf9]] - hChk Wnk1 kinase domain + inhibitor + AMPPNP 
**[[5wdy]], [[5we8]] - hChk Wnk1 kinase domain + inhibitor + ANP 
**[[5drb]], [[6ol2]]- rChk Wnk1 kinase domain (mutant) + inhibitor 
**[[6elm]] - hChk Wnk2 CCT1 domain 
**[[6fbk]] - hChk Wnk2 CCT1 domain + Wnk1 peptide 
**[[5o1v]], [[5o21]], [[5o23]] - hChk Wnk3 kinase domain 
**[[5o2c]] - hChk Wnk3 kinase + CCT1 domains 
**[[5o26]], [[5tf9]] - hChk Wnk3 kinase domain + AMPPNP 
**[[5o2b]] - hChk Wnk3 kinase domain + inhibitor 
**[[8edh]] - hChk Wnk3 kinase domain (mutant) + inhibitor 
**[[2lru]] – rChk Wnk1 autoinhibitory domain 480-572 - NMR 
**[[5w7t]] - rChk Wnk1 kinase domain 
**[[7uos]] - rChk Wnk1 kinase domain (mutant) 

*'''TANK-binding kinase'''

**[[4efo]] – hChk Tbk1 ubiquitin-like domain 
**[[6rsr]], [[6rsu]] – hChk Tbk1 + inhibitor 
**[[4im0]], [[4im2]], [[4im3]], [[4iw0]], [[4iwo]], [[4iwp]], [[4ipq]], [[6rst]] – hChk Tbk1 (mutant) + inhibitor 
**[[6cq5]], [[6cq4]], [[6cq0]], [[6boe]], [[6bod]], [[6bny]], [[5w5v]] – hChk Tbk1 + ulcer drug 
**[[4eut]], [[4euu]] – hChk Tbk1 kinase+ubiquitin-like domains (mutant) + inhibitor 
**[[6nt9]] – hChk Tbk1 (mutant) + STING 
**[[5eoa]], [[5eof]] – hChk Tbk1 residues 677-729 + optineurin 
**[[4jl9]], [[4jlc]] – mChk Tbk1 + inhibitor 
**[[6o8c]], [[6o8b]] – mChk Tbk1 (mutant) + STING 

*'''Haspin'''

**[[2vuw]], [[2wb8]] – hChk Haspin kinase domain 
**[[3dle]] – hChk Haspin kinase domain + AMP 
**[[3e7v]], [[3f2n]], [[3fmd]], [[3iq7]], [[4qtc]], [[5htb]], [[5htc]], [[6z56]], [[6z57]], [[6z58]], [[6z59]], [[6z5a]], [[6z5b]], [[6z5c]]. [[6z5d]], [[6z5e]] , [[7avq]], [[7ops]] – hChk Haspin kinase domain + inhibitor 
**[[7sqm]] – hChk Haspin kinase domain + antimalarial 
**[[6g38]], [[6g34]], [[6g35]], [[6g36]], [[6g37]] – hChk Haspin kinase domain + tubercidin derivative 
**[[6g39]], [[6g3a]] – hChk Haspin kinase domain (mutant) + tubercidin derivative 
**[[4ouc]] – hChk Haspin kinase domain + histone H3 peptide 

*'''MAP/microtubule affinity-regulating kinase (MARK)'''

**[[2hak]] – hChk MARK1 catalytic+UBA domains 
**[[3ose]] - hChk MARK1 KA1 domain 
**[[6c9d]] – hChk MARK1 catalytic+UBA+KA1 domains (mutant) 
**[[5eak]], [[5kz7]], [[5kz8]] – hChk MARK2 catalytic+UBA domains + inhibitor 
**[[3iec]] – hChk MARK2 catalytic+UBA domains + cytotoxicity-associated immunodominant antigen peptide 
**[[2qnj]] – hChk MARK3 catalytic+UBA domains 
**[[3fe3]] – hChk MARK3 catalytic+UBA domains (mutant) 
**[[7p1l]] – hChk MARK3 catalytic+UBA domains + inhibitor 
**[[5es1]] – hChk MARK4 catalytic+UBA domains + inhibitor 
**[[1zmu]] – rChk MARK2 catalytic+UBA domains 
**[[2wzj]], [[2r0i]], [[1zmv]], [[1y8g]], [[1zmw]] – rChk MARK2 catalytic+UBA domains (mutant) 
**[[1ul7]], [[1v5s]] - mChk MARK3 catalytic domain - NMR 

*'''Mitotic checkpoint Chk (Bub)'''; Domains: TPR 1-220; kinase 726-1085

**[[2lah]] – hChk Bub1 TPR domain – NMR 
**[[2wvi]] – hChk Bub1β TPR domain 
**[[3si5]] – hChk Bub1 TPR domain + CASC5 peptide 
**[[4r8q]], [[4qpm]], [[5dmz]] – hChk Bub1 kinase domain + ADP 
**[[6f7b]] – hChk Bub1 kinase domain + inhibitor 
**[[4a1g]] – hChk Bub1 TPR domain + CASC5 KI motif 
**[[4ggd]] - hChk Bub1 + cell division cycle protein 
**[[6tlj]], [[5khu]] - hChk Bub1 in anaphase-promoting complex – Cryo EM 
**[[6jkk]] – DmChk Bub1 kinase domain 
**[[6jkm]] – DmChk Bub1 kinase domain + ADP 
**[[5jja]] – hChk Bub1 residues 661-734 + PP2A 
**[[3esl]] – yChk Bub1 N terminal 
**[[4bl0]] - yChk Bub1 + cell cycle arrest protein Bub3 

*'''Microtubule-associated Chk'''

**[[2m9x]] – hChk 1 residues 187-287 – NMR 
**[[3ps4]] - hChk 1 residues 965-1057 
**[[2kqf]], [[2kyl]] – hChk 2 PDZ domain + glycoprotein C terminal – NMR 
**[[3khf]] - hChk 3 PDZ domain 
**[[2w7r]] – hChk 4 PDZ domain 

*'''mTOR''' or '''Mechanistic target of rapamycin'''

*''mTOR FRB domain residues 2015-2114''

**[[1nsg]], [[1fap]] – hFRAP FRB domain + FKBP 
**[[2rse]] – hFRAP FRB domain + FKBP – NMR 
**[[1aue]] – hFRAP FRB domain 
**[[2gaq]], [[2npu]] – hFRAP FRB domain - NMR 
**[[8ppz]] – hFRAP FRB domain + FKBP + pyridine derivative 
**[[3fap]], [[2fap]], [[4fap]] – hFRAP FRB domain + FKBP + rapamycin analog 
**[[4drh]], [[4dri]], [[4drj]], [[5gpg]] – hFRAP FRB domain + FKBP + rapamycin 
**[[6m4u]], [[6m4w]] – hChk Mtor FRB domain (mutant) + FKBP1A + rapamycin 
**[[5wbh]] – hFRAP FRB domain + S6K1 peptide 

*''mTOR FAT+PIKK domain residues 1376-2549''

**[[4jsn]] – hFRAP + TORC subunit LST8 
**[[4jsp]] – hFRAP + TORC subunit LST8 + ATP 
**[[4jsv]] – hFRAP + TORC subunit LST8 + ADP 
**[[4jsx]] – hFRAP + TORC subunit LST8 + torin2 
**[[4jt5]] – hFRAP + TORC subunit LST8 + pp242 
**[[4jt6]] – hFRAP + TORC subunit LST8 + PI-103 
**[[5wby]], [[5wbu]] – hFRAP + TORC subunit LST8 + proline-rich Akt1 substrate 

*''mTOR complex''

**[[5flc]] – hmTOR + RAPTOR + LST8 + FKBP – Cryo EM 
**[[5h64]] – hmTOR + RAPTOR + LST8 – Cryo EM 
**[[6sb2]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC – Cryo EM 
**[[6sb0]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC + proline-rich Akt1 substrate – Cryo EM 
**[[5zcs]] – hmTOR + LST8 + AVO3 + TORC2 – Cryo EM 
**[[7tzo]] – hTORC2 in mTORC2 complex– Cryo EM 
**[[6zwm]], [[6zwo]], [[7owg]], [[7pe7]], [[7pe8]], [[7pe9]], [[7pea]], [[7peb]], [[7pec]], [[7uxc]] , [[8era]]– mTOR in mTor complex – Cryo EM 

*'''Gcn2'''

**[[1zyc]] – yChk Gcn2 
**[[1zxe]], [[1zy4]], [[1zy5]] – yChk Gcn2 (mutant) 
**[[2yz0]] – yChk Gcn2 RWD/GI domain – NMR 
**[[4otm]] – yChk Gcn2 C terminal domain 
**[[1zyd]] – yChk Gcn2 + ATP 
**[[4otn]] – mChk Gcn2 C terminal domain 

*'''LRRK1''' or leucine-rich repeat Chk1

**[[8e04]], [[8e05]], [[8e06]], [[8fac]] – hLRRK1 – Cryo EM 

*'''LRRK2''' or leucine-rich repeat Chk2 or dardarin

**[[6xr4]] – hLRRK2 – Cryo EM 
**[[7lht]], [[7lhw]], [[7li4]] – hLRRK2 + ATP + GDP – Cryo EM 
**[[7li3]] – hLRRK2 (mutant) + ATP + GDP – Cryo EM 
**[[6oje]], [[7thy]] – hLRRK2 GTPase domain 1329-1520 
**[[6ojf]] – hLRRK2 GTPase domain (mutant) 
**[[6dlo]], [[6dlp]] – hLRRK2 WD40 domain 
**[[7thz]] – hLRRK2 1330-1527 + GDP 
**[[6vno]], [[6vp6]], [[6vp7]] – hLRRK2 C terminal 1330-2527 – Cryo EM 
**[[6vp8]] – hLRRK2 C terminal 1330-2527 + COR domain 1670-1950 + WD40 domain 2140-2489 – Cryo EM 
**[[6s6q]] – AtLRRK2 ectodomain + protein casparian strip peptide 

*'''Pim'''

*Pim1 catalytic domain residues 14-313

**[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain 
**[[1yxs]] – hPim1 catalytic domain (mutant) 
**[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP 
**[[1yxu]] – hPim1 catalytic domain + AMP 
**[[1yxv]], [[5ipj]] – hPim1 catalytic domain + quinoline derivative 
**[[1yxx]] – hPim1 catalytic domain + indole derivative 
**[[2bzh]], [[2bzi]], [[2bzj]] – hPim1 catalytic domain (mutant) + organometallic ligand 
**[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3c4e]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umw]], [[3umx]], [[4enx]], [[4eny]], [[4k1b]], [[4k18]], [[4k0y]], [[4iaa]], [[4i41]], [[4ll5]], [[4lm5]], [[4lmu]], [[4mta]], [[4med]], [[4mbl]], [[4mbi]], [[4n6y]], [[4n6z]], [[4n70]], [[4xh6]], [[5iis]], [[5kgd]], [[5kge]], [[5kgg]], [[5kgi]], [[5kgk]], [[5kzi]], [[5vua]], [[5vub]], [[5vuc]], [[6mt0]], [[6vrv]], [[7oov]], [[7oow]], [[7oox]], [[7xsv]] – hPim1 catalytic domain + inhibitor 
**[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor 

*Pim1 kinase domain residues 92-404

**[[4jx3]] – hPim1 kinase domain 
**[[3uix]], [[5c1q]] – hPim1 kinase domain residues 120-404 + quinoline derivative 
**[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate 
**[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand 
**[[1xws]], [[4alu]], [[4alv]], [[4alw]], [[4as0]], [[4bzn]], [[4bzo]], [[4dtk]], [[4jx7]], [[4rbl]], [[4rc2]], [[4rc3]], [[4rc4]], [[4ty1]], [[4wrs]], [[4wsy]], [[4wt6]], [[4xhk]], [[5dgz]], [[5dhj]], [[5dia]], [[5dwr]], [[5eol]], [[5kcx]], [[5o11]], [[5o12]], [[5o13]], [[5tel]], [[5tex]], [[5toe]], [[5v80]], [[5v82]]. [[6bsk]], [[6kzi]], [[6l11]], [[6l12]], [[6l13]], [[6l14]], [[6l15]], [[6l16]], [[6l17]], [[6no8]], [[6no9]], [[6vru]], [[6ykd]], [[7zun]] – hPim1 kinase domain + inhibitor 
**[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor 

*Pim1 full length

**[[4rpv]], [[5tur]] - hPim1 + inhibitor 

*Pim1 complex with consensus peptide (pimtide)

**[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6qxk]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]] – hPim1 kinase domain + inhibitor + consensus peptide 
**[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide 
**[[2c3i]], [[5ndt]], [[5n5m]], [[5n5l]], [[5n52]], [[5n51]], [[5n50]], [[5n4z]], [[5n4y]], [[5n4x]], [[5n4v]], [[5n4u]], [[5n4r]], [[5n4o]], [[5n4n]], [[5mzl]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide 
**[[4gw8]], [[7qb2]], [[7qfm]], [[7z6u]], [[8afr]] – hPim1 catalytic domain (mutant) + inhibitor + pimtide 
**[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide 
**[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide 

*Pim1 containing phosphorylated Ser 261

**[[1yhs]] – hPim1 kinase domain + PSer + staurosporine 
**[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor 
**[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor 
**[[1yi4]] – hPim1 kinase domain + PSer + adenosine 

*Pim2

**[[4x7q]] – hPim2 catalytic domain + inhibitor 
**[[2iwi]] – hPim2 catalytic domain + Ru ligand 

*'''Rip or receptor-interacting Chk; Domains – catalytic 1-294; Amyloid fibril 418-518; Death 561-671'''

**[[6ac5]] – hRip1 death domain 
**[[6r5f]], [[6nw2]], [[6c4d]], [[6c3e]], [[5tx5]], [[7fcz]], [[7fd0]], [[7ydx]] – hRip1 catalytic domain + inhibitor 
**[[6rln]], [[6ocq]], [[6nyh]], [[6hho]] – hRip1 catalytic domain (mutant) + inhibitor 
**[[6ggs]] – hRip2 – Cryo EM 
**[[5yrn]] – hRip2 CARD domain 434-540 – Cryo EM 
**[[6szj]], [[6sze]], [[6s1f]], [[6rna]], [[6rn8]], [[6hmx]], [[6fu5]], [[6es0]], [[5w5o]], [[5w5j]] – hRip2 catalytic domain + inhibitor 
**[[6ul8]] – hRip2 catalytic domain (mutant) + inhibitor 
**[[8aza]] – hRip2 catalytic domain + XiaP Bir2 domain – Cryo EM 
**[[7mx3]] – hRip3 catalytic domain (mutant) + inhibitor 
**[[7mon]] – hRip3 catalytic domain (mutant) + MLKL 
**[[7dac]] – hRip3 amyloid fibril - NMR 
**[[7da4]] – hRip3 amyloid fibril – Cryo EM 
**[[6oko]] – mRip3 catalytic domain + inhibitor 
**[[6jpd]] – mRip3 residues 409-486 - NMR 
**[[5wnm]], [[5wnj]] – mRip4 catalytic domain (mutant) + drug 
**[[5wnl]] – mRip4 catalytic domain (mutant) + staurosporine 
**[[5wnk]] – mRip4 catalytic domain (mutant) + inhibitor 
**[[5wni]] – mRip4 catalytic domain (mutant) + ATP 
**[[6gwm]] – rRip2 caspase recruitment domain 433-539 

*'''Ulk'''

**[[6qas]] – hChk Ulk1 + inhibitor 
**[[5ci7]], [[6mnh]] – hChk Ulk1 (mutant) + inhibitor 
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog 
**[[8soi]], [[8sqz]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein 
**[[8srm]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein – Cryo EM 
**[[8srq]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein + PI3K – Cryo EM 
**[[6qav]], [[6qau]], [[6qat]], [[6yid]] – hChk Ulk2 + inhibitor 
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor 
**[[6fdz]], [[6fdy]] – hChk Ulk3 + leukemia drug 
**[[6tsz]] – hChk Ulk4 pseudfokinase domain + ATPgS 
**[[6u5l]] – hChk Ulk4 (mutant) + inhibitor 

*'''Hipa''' and '''Hipb'''

**[[3tpd]], [[3tpe]] – EcChk Hipa – ''Escherichia coli'' 
**[[3tpb]], [[3dnt]], [[3dnu]] – EcChk Hipa (mutant) 
**[[4pu7]], [[4pu8]] – SoChk Hipb - ''Shewanella oneidensis'' 
**[[3tpt]] – EcChk Hipa (mutant) + ADP 
**[[3fbr]] – EcChk Hipa (mutant) + AMPPNP + peptide 
**[[3tpv]] – EcChk Hipa + ADP 
**[[2wiu]] – EcChk Hipa + Hipb 
**[[4yg7]], [[5k98]], [[3hzi]], [[3dnv]] – EcChk Hipa + Hipb + DNA 
**[[4yg1]], [[4z58]], [[4z59]], [[4z5c]], [[4z5d]] – EcChk Hipb + DNA 
**[[4z5h]] – EcChk Hipb (mutant) + DNA 
**[[4pu3]], [[4pu4]] – SoChk Hipa + Hipb + DNA - ''Shewanella oneidensis'' 
**[[4pu5]] – SoChk Hipa + AMPPNP 

*'''Chk Smg'''

**[[6l53]] – hChk Smg1 – Cryo EM 
**[[7pw6]] – hChk Smg1 + inhibitor – Cryo EM 
**[[7pw7]] – hChk Smg1 + Smg9 + inhibitor – Cryo EM 
**[[7pw9]] – hChk Smg1 + Smg9 + AMPPNP + ATP – Cryo EM 
**[[6l54]], [[6syt]] – hChk Smg1 + Smg8 + Smg9 – Cryo EM 
**[[7pw4]], [[7pw5]] – hChk Smg1 + Smg8 + Smg9 + inhibitor – Cryo EM 
**[[7pw8]] – hChk Smg1 + Smg8 + Smg9 + AMPPNP – Cryo EM 
**[[6z3r]] – hChk Smg1 + Smg8 + Smg9 + regulator of nonsense transcripts – Cryo EM 
**[[2hwy]] – hChk Smg5 PIN domain 
**[[2hww]], [[2hwx]] – hChk Smg6 PIN domain (mutant) 
**[[4um2]] – hChk Smg6 TPR domain 
**[[1ya0]] – hChk Smg7 N terminal 

*'''Chk Vprbp or DCAF1'''

**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain 1039-1401 (mutant) 
**[[7sse]], [[7ufv]], [[8f8e]], [[8og5]], [[8og6]], [[8og7]], [[8og8]], [[8og9]], [[8oga]], [[8ogb]], [[8ogc]], [[8oo5]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) + inhibitor 
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM 
**[[5aja]] – hChk Vprbp WD repeat domain + VPX + SAMHD1 

*'''Other Chk'''

**[[1wak]] – hChk Sprk1 
**[[3dak]] – hChk Osr1 kinase domain 
**[[7okw]] – hChk Osr1 C-terminal 
**[[4aw2]] – hChk Mrckα kinase domain 
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) 
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM 
**[[1uf0]] – hChk Dcamkl1 DCX domain – NMR 
**[[1u5q]] – rChk Tao2 kinase domain 
**[[2cos]] – mChk Lats2 – NMR 
**[[1xte]], [[1xtn]], [[6edx]] – mChk Sgk3 PX domain 
**[[4yom]] – mChk Brsk2 
**[[4ynz]] – mChk Brsk1 N terminal domain 
**[[5iri]] – mChk Brsk1 residues 592-719 
**[[5oat]], [[7mp8]] – rfbChk Pink1– red flour beetle 
**[[7t3x]] – Chk Pink1 (mutant) – louse 
**[[4f0g]] – smChk Roco4 kinase domain – slime mold 
**[[5tos]] – AtChk Bik1 
**[[1q8z]], [[1zyc]] – yChk 
**[[1how]], [[1zxe]], [[1zy4]] – yChk (mutant) 
**[[1ow5]], [[1x9x]] – yChk Ste11 SAM domain – NMR 
**[[2kio]], [[2kit]], [[1w1n]] – yChk Tor1 FATC domain – NMR 
**[[3gre]] – yChk Vps15 WD repeat domain 
**[[3osm]], [[3ost]] - yChk Kcc4 kinase domain 
**[[5yyx]] – yChk Mek1 FHA domain 
**[[6jxc]], [[6jxa]] – yChk Tel1 – Cryo EM 
**[[6u69]] – CaChk Yck2 – ''Candida albicans'' 
**[[6sl1]], [[6sl0]], [[6skz]], [[6sky]] – Chk Tel1 – ''Chaetonium thermophilum'' – Cryo EM 
**[[6ra0]] – CeChk Dkf1 – ''Chaenorhabditis elegans'' 
**[[7z6e]] – CeChk Mrck1 regulatory domain 
**[[6tlb]] – Chk – ''Plasmodium falciparum'' 

*Other Chk complexes

**[[1wbp]], [[7dd1]] – hChk Sprk1 + peptide 
**[[3beg]] – hChk Srpk1 + splicing factor SF2 
**[[3hdm]], [[3hdn]], [[7pue]] – hChk Sgk1 (mutant) + inhibitor 
**[[2r5t]] – hChk Sgk3 + AMPPNP 
**[[4yff]], [[4yfi]], [[6b5j]], [[7mgj]], [[7mgk]] – hChk Tnni3k + inhibitor 
**[[2v3s]] – hChk Osr1 + hChk Wnk4 peptide 
**[[2vwi]] – hChk Osr1 kinase domain + ANP 
**[[7que]], [[7quf]] – hChk Drak1 kinase domain + inhibitor 
**[[4crs]] – hChk N2 kinase domain + ATPγS 
**[[3tku]], [[4ual]], [[3qfv]], [[5ote]], [[5otf]] – hChk Mrckβ + inhibitor 
**[[4uak]] – hChk Mrckβ + ADP 
**[[5aja]], [[4z8l]], [[4cc9]] – hChk Vprbp WD repeat domain + VPX + SAMHD1 
**[[5jk7]] – hChk Vprbp WD repeat domain + VPX + DDB1 + UDG 
**[[3wa0]], [[4p7i]] – hChk Vprbp residues 1417-1506 + merlin 
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor 
**[[5ci7]] – hChk Ulk1 (mutant) + inhibitor 
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog 
**[[5b5w]], [[5b6b]], [[5brk]] – hChk Lats1 residues 622-704 + MOB1 
**[[5yz0]] – hChk Atr + Atr-interacting protein – Cryo EM 
**[[6bdn]] – hChk Tao3 kinase domain + ADP 
**[[5yh3]] – hChk Fam20C 141-578 + pseudokinase Fam20A 
**[[2gcd]] – rChk Tao2 kinase domain + staurosporine 
**[[1u5r]] – rChk Tao2 kinase domain + ATP 
**[[5yj9]], [[7mp9]] – rfbChk Pink1 kinase domain + AMPPNP 
**[[6bn1]] – DmChk Hippo SARAH domain + Shar-Pei 
**[[3hgk]] – Chk Pto + effector protein AVRPTOB – Currant tomato 
**[[3p86]], [[3ppz]] - AtChk Ctr1 + staurosporine 
**[[4f0f]] – smChk Roco4 kinase domain + APPCP 
**[[4f1m]], [[4f1o]] – smChk Roco4 kinase domain (mutant) + APPCP 
**[[4f1t]], [[4yzm]], [[4yzn]] – smChk Roco4 kinase domain + inhibitor 
**[[5fvm]] - Tor2 + LST8 - ''Kluyveromyces marxianus'' 
**[[5kc2]] - yVps15 + Vps34 - Cryo EM 
**[[5dfz]] - yVps15 + Vps34 + Vps30 + VPSAP28 + VPSAP30 - Cryo EM 
**[[1q8y]], [[1q97]], [[1q99]], [[1zyd]] – yChk + nucleotide 
**[[1zy5]] – yChk (mutant) + nucleotide 
**[[2jd5]] – yChk + NPL-3P 
**[[4lqs]], [[4lqq]], [[4lqp]] – yChk Cbk1 residues 251-756 + Cbk1 activator Mob2 
**[[6emk]] – yChk Tor2 + LST8 + TSC11 + AVO1 + AVO2 – Cryo EM 
**[[6s8f]] – yChk Tel1 + AMPPNP – Cryo EM 
**[[5yyz]] – yChk Mek1 FHA domain + Hop1 
**[[5x6o]], [[6z3a]], [[7wzr]], [[7wzw]]– yChk Mec1 + LCD1 – Cryo EM 
**[[6z2w]], [[6z2x]] – yChk Mec1 (mutant) + LCD1 – Cryo EM 
**[[7kue]] – yChk Kin28 in TFIIK complex – Cryo EM 
**[[6u6a]] – CaChk Yck2 + inhibitor 
**[[5fvm]] – Chk Tor2 + LST8 – ''Kluyveromyces maximanus'' 

*Serine/threonine protein kinase Rad53 see [[Rad53]]

*Serine/threonine protein kinase Gsk3B see [[Glycogen synthase kinase 3]]

}}

[[Category:Topic Page]]

Serine/threonine protein kinase 3D structures

2026-08-16T10:39:02Z

Michal Harel:

==3D structures of serine/threonine protein kinase==

Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

*'''Chk1'''; domains - kinase 1-289; KA1 393-492

**[[1ia8]] – hChk1 kinase domain – human 
**[[5w12]] – hChk1 KA1 domain 
**[[1zlt]] – hChk1 kinase domain + hymenaldisine 
**[[1nvq]], [[1nvr]] – hChk1 kinase domain + peptide + saurosporine

**[[1nvs]], [[1zys]], [[7ako]] - hChk1 kinase domain + peptide + inhibitor
**[[7akm]] - hChk1 kinase domain + ATP 
**[[2cgu]], [[2cgv]], [[2cgw]], [[2cgx]], [[2c3j]], [[2c3k]], [[2c3l]], [[2br1]], [[2brb]], [[2brg]], [[2brh]], [[2brm]], [[2brn]], [[2bro]], [[2ayp]], [[2gdo]], [[2ghg]], [[2hog]], [[2ywp]], [[2hxl]], [[2hxq]], [[2hy0]], [[2r0u]], [[2e9n]], [[2e9o]], [[2e9p]], [[2e9u]], [[2e9v]], [[2qhm]], [[2qhn]], [[3f9n]], [[2wmq]], [[2wmr]], [[2wms]], [[2wmt]], [[2wmu]], [[2wmv]], [[2wmx]], [[3jvr]], [[3jvs]], [[2xey]], [[2xf0]], [[2xez]], [[2x8d]], [[2x8e]], [[2x8i]], [[3ot3]], [[3ot8]], [[3pa3]], [[3pa4]], [[3pa5]], [[3nlb]], [[2wmw]], [[2ydi]], [[2ydj]], [[2ydk]], [[2yer]], [[2yex]], [[2ym3]], [[2ym4]], [[2ym5]], [[2ym6]], [[2ym7]], [[2ym8]], [[3tkh]], [[3tki]], [[3u9n]], [[4fsm]], [[4fsn]], [[4fsq]], [[4fsr]], [[4fst]], [[4fsu]], [[4fsw]], [[4fsy]], [[4fsz]], [[4ft0]], [[4ft3]], [[4ft5]], [[4ft7]], [[4ft9]], [[4fta]], [[4ftc]], [[4fti]], [[4ftj]], [[4ftk]], [[4ftl]], [[4ftm]], [[4ftn]], [[4fto]], [[4ftq]], [[4ftr]], [[4ftt]], [[4ftu]], [[4gh2]], [[4hyh]], [[4hyi]], [[4jik]], [[4rvm]], [[4rvl]], [[4rvk]], [[4qyh]], [[4qyg]], [[4qyf]], [[4qye]], [[5dls]], [[5f4n]], [[6fc8]], [[5fcf]], [[5fck]], [[6fck]], [[6fcf]], [[7bko]], [[8e80]], [[8e81]] - hChk1 kinase domain + inhibitor 
**[[5oot]], [[5op2]], [[5op4]], [[5op5]], [[5op7]], [[5opb]], [[5opr]], [[5ops]], [[5opu]], [[5opv]], [[5oq5]], [[5oq6]], [[5oq7]], [[5oq8]], [[7bjd]], [[7bjh]], [[7bjj]], [[7bjm]], [[7bjo]], [[7bjr]], [[7bjx]], [[7bk1]], [[7bk2]], [[7bk3]], [[7mck]], [[7suf]], [[7sug]], [[7suh]], [[7sui]], [[7suj]], [[8siv]], [[8siw]], [[8six]] - hChk1 kinase domain (mutant) + inhibitor 
**[[5oop]] - hChk1 kinase domain (mutant) + AMPPNP 
**[[5oor]] - hChk1 kinase domain (mutant) + staurosporine 
**[[7bkn]] - hChk1 kinase domain + adenine 
**[[7bje]] - hChk1 kinase domain (mutant) + adenine 
**[[2jqi]] – yChk1 – yeast 

*'''Chk2 (Checkpoint kinase)'''

**[[1gxc]] – hChk2 phosphothreonine-binding domain + phosphopeptide 
**[[2cn5]] – hChk2 kinase domain + ADP 
**[[2cn8]] – hChk2 kinase domain + inhibitor 
**[[2w0j]], [[2w7x]], [[2wtc]], [[2wtd]], [[2xbj]], [[2xm8]], [[2xm9]], [[2yiq]], [[2yir]], [[2yit]], [[2cn8]], [[2ycf]], [[2ycq]], [[2ycr]], [[2ycs]], [[2wti]], [[2wtj]], [[2xk9]], [[4a9r]], [[4a9s]], [[4a9t]], [[4bda]], [[4bdb]], [[4bdc]], [[4bdd]], [[4bde]], [[4bdf]], [[4bdg]], [[4bdh]], [[4bdi]], [[4bdj]], [[4bdk]], [[2uv2]] - hChk2 kinase domain + inhibitor 
**[[3i6u]], [[3i6w]] – hChk2 residues 84-502 (mutant)

*'''Chk3 (Mst2)'''; domains - kinase 13-313; SARAH 436-484

**[[4hkd]], [[4l0n]], [[4oh9]], [[3wws]] – hChk3 SARAH domain 
**[[4lg4]] – hChk3 kinase domain 
**[[4lgd]] – hChk3 kinase domain + RASSF5 SARAH domain 
**[[6ao5]] – hChk3 kinase+SARAH domains (mutant) + SAV1 SARAH domain 
**[[5dh3]], [[8a66]] – hChk3 kinase domain + inhibitor 

*'''Chk4 (Mst1)''' ; Domains – kinase 1-311; SARAH 432-480

**[[3com]] – hChk4 kinase domain 
**[[6yat]], [[8a5j]]– hChk4 kinase domain + inhibitor 
**[[4nr2]] – hChk4 SARAH domain 
**[[2jo8]] – hChk4 SARAH domain - NMR 
**[[4oh8]] – hChk4 SARAH domain + Ras association domain-containing protein 

*'''Chk5 (Aurora kinase b)'''

**[[4af3]] – hChk5 + inhibitor 

*'''Chk6 or Chk15 or Aurora kinase A'''

**[[1muo]], [[1mq4]], [[4j8n]], [[6cpe]], [[4o0s]] – hChk6 kinase domain 
**[[4bn1]], [[4o0w]], [[4o0u]] – hChk6 kinase domain (mutant) 
**[[5dnr]], [[5drd]], [[5dt3]] – hChk6 kinase domain + ATP 
**[[5drd]] – hChk6 kinase domain + ATP 
**[[1ol6]] – hChk6 kinase domain (mutant) + ATP 
**[[2wqe]] – hChk6 kinase domain (mutant) + ADP 
**[[5odt]] – hChk6 kinase domain (mutant) + ADP + TACC3 
**[[2c6d]] – hChk6 kinase domain (mutant) + ADPNP 
**[[2dwb]] – hChk6 kinase domain + AMPPNP 
**[[6cpf]] – hChk6 kinase domain + AMPPCP 
**[[5g15]] – hChk6 kinase domain + AMPPNP + monobody 
**[[6cpg]], [[8ssp]] – hChk6 kinase domain + inhibitor + monobody 
**[[2j4z]], [[2j50]], [[2np8]], [[3efw]], [[2x81]], [[2x6d]], [[2x6e]], [[3myg]], [[3vap]], [[4b0g]], [[4j8m]], [[5dpv]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5one]], [[5obr]], [[4byi]], [[4byj]], [[4jai]], [[4jaj]], [[3w10]], [[3w16]], [[3w18]], [[3w2c]], [[4uzh]], [[4uzd]], [[4uyn]], [[4zs0]], [[4ztq]], [[4ztr]], [[4zts]], [[5aad]], [[5aae]], [[5aag]], [[5dr6]], [[5dr9]], [[5dt0]], [[5ew9]], [[5obr]], [[5one]], [[6gra]], [[6c2t]], [[6c2r]], [[5zan]], [[6z4y]], [[7ayh]], [[7ayi]], [[7fic]], [[7o2v]], [[8jmx]] – hChk6 kinase domain + inhibitor 
**[[2bmc]], [[2c6e]], [[3coh]], [[3h0y]], [[3h0z]], [[3h10]], [[3fdn]], [[2wtw]], [[3lau]], [[3nrm]], [[2xne]], [[2xng]], [[2xru]], [[3k5u]], [[3m11]], [[3p9j]], [[3r21]], [[3r22]], [[3qbn]], [[3unz]], [[3uo4]], [[3uo5]], [[3uo6]], [[3uod]], [[3uoh]], [[3uoj]], [[3uok]], [[3uol]], [[3up2]], [[3up7]], [[4dhf]], [[4dea]], [[4deb]], [[4ded]], [[4dee]], [[5aad]], [[5aae]], [[5aaf]], [[5aag]], [[4jbo]], [[4jbp]], [[4jbq]], [[4prj]], [[5dpv]], [[6hjk]], [[6hjj]] – hChk6 kinase domain (mutant) + inhibitor 
**[[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor 
**[[5dos]], [[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor 
**[[5dn3]], [[5dos]], [[5dt4]], [[5obj]] – hChk6 kinase domain + ATP + inhibitor 
**[[6c83]] – hChk6 kinase domain + AMPPCP + nanobody 
**[[8sso]] – hChk6 kinase domain + drug + monobody 
**[[5dr2]] – hChk6 kinase domain (mutant) + ATP + inhibitor 
**[[5g1x]], [[7ztl]] – hChk6 kinase domain (mutant) + N-Myc 
**[[8guw]] – hChk6 kinase domain/activator peptide 
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + new antigen receptor variable domain 
**[[5lxm]] – hChk6 kinase domain (mutant) + Targeting protein for XKLP2 
**[[3daj]], [[3d14]], [[3dj5]], [[3dj6]], [[3dj7]], [[3d15]], [[3d2i]], [[3d2k]] – Chk6 kinase domain (mutant) + inhibitor - mouse 

*Chk6 with phosphorylated Thr 287, Thr288

**[[1ol5]], [[1ol7]] – hChk6 kinase domain + PThr + ADP 
**[[5dnr]], [[5dt3]] – hChk6 kinase domain + PThr + ATP 
**[[2w1c]], [[2w1d]], [[2w1e]], [[2w1f]], [[2w1g]], [[5dn3]] – hChk6 kinase domain + PThr + inhibitor 
**[[2wtv]], [[5orl]], [[5orn]], [[5oro]], [[5orp]], [[5orr]], [[5ors]], [[5ort]], [[5orv]], [[5orw]], [[5orx]], [[5ory]], [[5orz]], [[5os0]], [[5os1]], [[5os2]], [[5os3]], [[5os4]], [[5os5]], [[5os6]], [[5osd]], [[5ose]], [[5osf]] – hChk6 kinase domain (mutant) + PThr + inhibitor 
**[[3e5a]], [[3ha6]] – hChk6 kinase domain + PThr + inhibitor + targeting protein for XKLP2 
**[[5g1x]] – hChk6 kinase domain (mutant) + PThr + N-Myc 
**[[5l8j]], [[5l8k]], [[5l8l]] – hChk6 kinase domain (mutant) + PThr + new antigen receptor variable domain 
**[[5lxm]] – hChk6 kinase domain (mutant) + PThr + TPX2 
**[[6r4d]], [[6r4c]], [[6r4b]], [[6r4a]] – hChk6 kinase domain + PThr + inhibitor + ADP 
**[[6i2u]] – hChk6 kinase domain (mutant) + PThr + inhibitor + ADP 
**[[6r49]] – hChk6 kinase domain (mutant) + PThr + CoA 

*'''Chk10 (lymphocyte-oriented kinase)''' or LOK or STK10

**[[7qgp]] – hChk10 
**[[2j7t]], [[4aot]], [[4equ]], [[4usd]], [[4use]], [[5ajq]], [[5owq]], [[5owr]], [[6eim]], [[6gtt]], [[6i2y]], [[6hxf]] – hChk10 kinase domain + inhibitor 
**[[4bc6]], [[6i2y]] – hChk10 + drug 

*'''Chk11'''

**[[2wtk]] – hChk11 (mutant) + calcium-binding protein 

*'''Chk12-A (Aurora kinase b-a or Aurora B kinase)'''

**[[2vgo]], [[2vgp]], [[2vrx]], [[3ztx]], [[4c2v]], [[5eyk]] – fChk12-A + inner centromere protein A peptide + inhibitor - frog 
**[[4c2w]] – fChk12-A + inner centromere protein A peptide + AMPPNP 
**[[4b8l]], [[4b8m]], [[5k3y]] – fChk12-A (mutant) + inner centromere protein A peptide + inhibitor 

*'''Chk13 (Polo-like kinase Plk)'''

*Plk1 Polo-box domain (Pbd) 371-594''

**[[1q4o]], [[2ogq]], [[3hih]], [[3p2w]], [[4h5x]], [[6n46]] – hPlk1 Pbd 

*Plk1 Pbd complex with polypeptide

**[[1umw]], [[2ojx]], [[3bzi]], [[3c5l]], [[3rq7]], [[4dfw]], [[4whl]], [[4whk]], [[4whh]], [[4rcp]], [[4o6w]], [[4o56]], [[5dms]], [[5dmv]], [[5dnj]] , [[7mso]], [[7mx1]] – hPlk1 + peptide 
**[[3hik]], [[3fvh]], [[3p2z]], [[3p34]], [[3p35]], [[3p36]], [[3p37]], [[3q1i]], [[4e67]], [[4e9c]], [[4e9d]], [[4hab]], [[4hy2]], [[4o9w]], [[4x9r]], [[4x9v]], [[4x9w]], [[5j19]], [[6gy2]] – hPlk1 + phosphopeptide 
**[[1q4k]] – hPlk1 (mutant) + phosphopeptide 
**[[2v5q]] – hPlk1 + design ankyrin repeat protein 
**[[4lkl]] – hChk Plk1 + PL-55 
**[[4lkm]] – hChk Plk1 + PL-74 
**[[6ax4]] – hChk Plk1 + histidine cyclized macrocycle 
**[[5x3s]] – mPlk1 + phosphopeptide 
**[[8joq]], [[8joy]] – hPlk1 Pbd + hpv peptide 

*Plk1 Pbd complex with small molecule inhibitor

**[[4h71]], [[4hco]], [[5ta6]], [[5ta8]], [[8bjt]], [[8crc]] – hPlk1 + inhibitor 
**[[2rku]] – hPlk1 (mutant) + inhibitor 
**[[3db6]], [[3db8]], [[3dbc]], [[3dbd]], [[3dbe]], [[3dbf]] – zfPlk1 (mutant) + inhibitor – zebra fish 

*Plk1 catalytic domain 36-345

**[[2owb]] – hPlk1 catalytic domain (mutant) 
**[[2ou7]] – hPlk1 catalytic domain (mutant) + AM
**[[3kb7]], [[2yac]], [[3thb]], [[4a4l]], [[4a4o]] – hPlk1 catalytic domain + inhibitor 
**[[3fc2]] – hPlk1 catalytic domain (mutant) + inhibitor 
**[[4j52]], [[4j53]] – hChk Plk1 (mutant) + inhibitor 
**[[3d5x]] – zfPlk1 catalytic domain (mutant) + wortmannin 
**[[3d5w]] – zfPlk1 catalytic domain + ADP 

*'''Plk2'''

**[[4i5m]], [[4i5p]], [[4i6b]], [[4i6f]], [[4i6h]] – hChk Plk2 kinase domain (mutant) + inhibitor 
**[[4xb0]], [[4rs6]] – hChk Plk2 Pbd 

*'''Plk3'''

**[[4b6l]], [[4i6b]] – hChk Plk3 kinase domain + inhibitor 

*'''Plk4'''; Domains – kinase 2-275; Pbd 580-808; Pb3 884-970

**[[3cok]] – hChk Plk4 kinase domain 
**[[4n9j]] – hChk Plk4 Pbd domain 
**[[4n7z]], [[4n7v]] – hChk Plk4 Pbd domain + centrosomal protein 
**[[6w38]], [[6w3i]] – hChk Plk4 Pbd domain + Fam46C 
**[[6w3j]] – hChk Plk4 Pbd domain + Fam46C + CEP92 peptide 
**[[4jxf]], [[4yur]] – hChk Plk4 kinase domain + inhibitor 
**[[5lhy]] – hChk Plk4 Pb3 domain 
**[[4yyp]], [[5lhz]] – hChk Plk4 Pb3 domain + Scl-interrupting locus protein 
**[[4nk7]], [[4g7n]], [[5lhx]], [[7rl3]] – DmChk Plk4 Pbd domain – ''Drosophila melanogaster'' 

*'''Chk16'''

**[[2buj]] – hChk16 (mutant) + staurosporin 

*'''Chk17B''' or DRAK2 or STK17B

**[[3lm0]] – hChk17B 
**[[6qf4]], [[7q7c]], [[7q7d]] – hChk17B + ADP 
**[[7q7e]] – hChk17B + ATP 
**[[3lm5]] – hChk17B + quercetin 
**[[6y6f]], [[6y6h]], [[6zjf]] – hChk17B + pyrimidine derivative 
**[[7akg]] – hChk17B + drug 

*'''Chk19''' or STK19

**[[7xrb]] – hChk19 

*'''Chk24 (Mst3)''' or STK24

**[[3a7f]], [[3a7g]], [[3a7h]], [[3a7i]], [[3a7j]], [[3ckw]] – hChk24 kinase domain 
**[[4w8e]], [[4w8d]], [[4u8z]], [[4qmm]], [[4qmn]], [[4qmo]], [[4qmp]], [[4qmq]], [[4qms]], [[4qmt]], [[4qmu]], [[4qmv]], [[4qmw]], [[4qmx]], [[4qmy]], [[4qmz]], [[4qna]], [[4qo9]], [[4u8z]], [[7b30]], [[7b31]], [[7b32]], [[7b33]], [[7b34]], [[7b35]], [[8bzi]], [[8bzj]], [[8qlr]], [[8qls]], [[8qlt]] – hChk Mst3 + inhibitor 
**[[8qlq]] – hChk Mst3 + macrocyclic inhibitor 
**[[3ckx]] – hChk24 kinase domain + staurosporin 
**[[3zhp]] – hChk24 kinase domain + calcium-binding protein 
**[[4o27]] – hChk24 kinase domain (mutant) + calcium-binding protein 
**[[4qml]] – hChk Mst3 kinase domain + AMPPNP 

*'''Chk25 or STK25'''

**[[2xik]] – hChk25 kinase domain 
**[[7z4v]] – hChk25 kinase domain + inhibitor 
**[[3w8h]] – hChk25 regulatory domain + programmed cell death protein 10 
**[[4nzw]] – hChk25 kinase domain (mutant) + calcium-binding protein 

*'''Chk26 (Mst4)'''

**[[3ggf]], [[7b36]] – hChk Mst4 + inhibitor 
**[[4geh]], [[3w8i]] - hChk Mst4 dimerization domain + programmed cell death protein 10 
**[[4fza]], [[4fzd]], [[4fzf]] – hChk Mst4 (mutant) + calcium-binding protein 

*'''Chk32'''

**[[4fr4]] – hChk32A 

*'''Chk38'''

**[[6bxi]] – hChk38 kinase domain 

*'''Chk39''' or SPAK

**[[7o86]] – hChk39 C-terminal 
**[[5d9h]] – mChk39 residues 63-403 + ATP 
**[[5dbx]] – mChk39 residues 63-403 (mutant) + AMPPNP 

*'''Chk40'''

**[[5l2q]] – hChk40 kinase homology domain 

*'''Dclk1'''

**[[6kyq]] – hChk Dclk1 kinase domain 
**[[6kyr]] – hChk Dclk1 kinase domain (mutant) 
**[[5jzj]] – hChk Dclk1 kinase domain + AMPPN 
**[[5jzn]], [[7kx6]], [[7kxw]] – hChk Dclk1 kinase domain + inhibitor 
**[[7f3g]] – hChk Dclk1 kinase domain + drug 
**[[7kx8]] – hChk Dclk1 C-terminal + inhibitor 

*'''Rac-α hChk (AKT1)'''; domains: pleckstrin homology 1-123; kinase 144-480

**[[1unp]], [[1unr]] – hRac-α hChk pleckstrin homology domain 
**[[2uzr]], [[2uzs]], [[7myx]] – hRac-α hChk pleckstrin homology domain (mutant) 
**[[1h10]], [[1unq]], [[2uvm]] – hRac-α hChk pleckstrin homology domain + inositol tetrakisphosphate 
**[[3o96]], [[4ejn]], [[6s9w]], [[6s9x]], [[6hhj]], [[6hhi]], [[6hhh]], [[6hhg]], [[6hhf]] - hRac-α hChk + inhibitor 
**[[5kcv]], [[7nh4]], [[7nh5]] - hRac-α hChk (mutant) + inhibitor 
**[[4gv1]], [[4ekl]] - hRac-α hChk kinase domain + inhibitor 
**[[3qkm]], [[6ccy]] - hRac-α hChk kinase domain (mutant) + inhibitor 
**[[6buu]] - hRac-α hChk kinase domain + bisubstrate peptide 
**[[4ekk]] - hRac-α hChk kinase domain (mutant) + GSK3 peptide + AMPPNP 
**[[6npz]] - hRac-α hChk kinase domain + peptide + inhibitor 
**[[3ow4]], [[3qkk]], [[3qkl]], [[6buu]] - hRac-α hChk kinase domain (mutant) + peptide + inhibitor 
**[[7apj]] - hRac-α hChk + nanobody 

*'''Rac-β hChk (AKT2)'''

**[[1gzk]], [[1gzn]], [[1gzo]], [[1mrv]], [[1mry]] – hRac-β hChk kinase domain 
**[[1p6s]] - hRac-β hChk pleckstrin homology domain - NMR 
**[[1o6k]] - hRac-β hChk kinase domain + GSK3 peptide + AMPPNP 
**[[2jdo]], [[2jdr]], [[2uw9]], [[2x39]], [[3cqu]], [[3cqw]] - hRac-β hChk kinase domain + GSK3 peptide + inhibitor 
**[[3e87]], [[3e88]], [[3e8d]] - Rac-β hChk kinase domain (mutant) + GSK3 peptide + inhibitor 
**[[3d0e]], [[8q61]] - hRac-β hChk kinase domain (mutant) + inhibitor 

*'''Rac-γ hChk (ATK3)'''

**[[2x18]] – Rac-γ hChk PH domain 

*'''A-Raf'''

**[[1wxm]] – hA-Raf RAS-binding domain 19-91 - NMR 
**[[2mse]] – hA-Raf RAS-binding domain + APOA-I + K-ras - NMR 

*'''B-Raf'''; domains - BRS 38-116; Ras-binding 153-237; kinase 445-723

**[[8dgs]], [[8dgt]] – hB-Raf in Ras/Raf complex – Cryo EM 
**[[7z37]], [[7z38]], [[7zr5]] – hB-Raf + Hsp90 + CDC37 + PP5 – Cryo EM 
**[[1uwh]], [[3c4c]], [[6v2u]], [[6xfp]], [[6xlo]], [[8f7o]], [[8f7p]] – hB-Raf kinase domain + anticancer drug 
**[[1uwj]], [[6p3d]] – hB-Raf kinase domain (mutant) + anticancer drug 
**[[2fb8]], [[3d4q]], [[3ii5]], [[3psd]], [[3skc]], [[3tv6]], [[4g9c]], [[4ksp]], [[4ksq]], [[3psb]], [[3ppj]], [[3ppk]], [[3prf]], [[3pri]], [[3tv4]], [[4dbn]], [[4e4x]], [[4mbj]], [[4ehe]], [[3q4c]], [[3q96]], [[3e26]], [[4h58]], [[4e26]], [[4fc0]], [[4pp7]], [[6cad]], [[7shv]] – hB-Raf kinase domain + pyrazole inhibitor 
**[[4jvg]], [[4ehg]], [[4fk3]], [[3idp]], [[4g9r]], [[4wo5]], [[4mnf]], [[4r5y]], [[4rzv]], [[4rzw]], [[4xv1]], [[4xv2]], [[4xv3]], [[4xv9]], [[4yht]], [[5c9c]], [[5hi2]], [[5ita]], [[5jrq]], [[5jsm]], [[5jt2]], [[6nsq]], [[6p7d]], [[6uuo]] – hB-Raf kinase domain (mutant) + pyrazole inhibitor 
**[[5csw]], [[5csx]], [[5ct7]], [[5fd2]], [[5hid]], [[5hie]], [[5val]], [[5vam]], [[6b8u]], [[6n0q]], [[6n0p]], [[7k0v]], [[7p3b]], [[7p3v]], [[8c7x]], [[8c7y]] - hB-Raf kinase domain + inhibitor 
**[[6v34]] – hB-Raf kinase domain (mutant) + inhibitor 
**[[4mne]] – hB-Raf kinase domain + MAPKK1 
**[[8f7o]] – hB-Raf kinase domain + drug 
**[[7m0u]] – hB-Raf kinase domain + AMPPNP + drug 
**[[6u2h]] – hB-Raf kinase domain + 14-3-3 ζ/δ 
**[[7mfe]] – hB-Raf + 14-3-3 ζ/δ – Cryo EM 
**[[7mff]] – hB-Raf + 14-3-3 ζ/δ + inhibitor – Cryo EM 
**[[7mfd]] – hB-Raf + 14-3-3 ζ/δ + MEK + inhibitor – Cryo EM 
**[[6pp9]] – hB-Raf kinase domain + MEK1 + ANP 
**[[7m0x]], [[7m0z]] – hB-Raf kinase domain + MEK1 + ANP + inhibitor 
**[[7m0t]], [[7m0u]], [[7m0v]], [[7m0w]], [[7m0y]] – hB-Raf kinase domain + MEK1 + ANP + drug 
**[[6u2g]] – hB-Raf kinase domain + MEK1 + AMPPCP 
**[[5vr3]] – hB-Raf BRS domain 
**[[7jhp]] – hB-Raf BRS domain + Hras 
**[[6ntc]], [[6ntd]] – hB-Raf BRS domain (mutant) + Hras 
**[[6xi7]] – hB-Raf 52-188 + Kras 
**[[2l05]], [[5j17]], [[5j2r]] – hB-Raf RAS-binding domain - NMR 
**[[3ny5]] – hB-Raf RAS-binding domain 
**[[5j18]] – hB-Raf RAS-binding domain + inhibitor - NMR 
**[[6pts]], [[6ptw]] – hB-Raf 56-187 + Kras + apolipoprotein + GMPPNP - NMR 
**[[6uan]], [[6q0k]] – hB-Raf + 14-3-3 ζ – Cryo EM 
**[[6nyb]] – hB-Raf + 14-3-3 ζ + MEK1 – Cryo EM 
**[[6q0t]], [[6q0j]] – hB-Raf (mutant) + 14-3-3 ζ + MEK1 – Cryo EM 

*'''c-Raf'''; Domains – RAS-binding (RBD) 55-132; Cys-rich 136-187 (CBD); kinase 323-618

**[[1rfa]], [[8jna]], [[8jof]], [[8jog]] – hc-Raf RBD - NMR 
**[[1faq]], [[1far]] – hc-Raf cysteine-rich domain - NMR 
**[[3omv]] – hc-Raf kinase domain 
**[[1rrb]] – c-Raf RBD – NMR - rat 

*c-Raf complex with protein

**[[8cpd]] – hc-Raf + 14-3-3 protein zeta – Cryo EM 
**[[9mmp]] – hc-Raf + MEK1 + 14-3-3 protein zeta – Cryo EM 
**[[9mmr]] – hc-Raf (mutant) + MEK1 + 14-3-3 protein zeta – Cryo EM 
**[[1c1y]] – hc-Raf RBD + RAP1A 
**[[3kuc]] – hc-Raf RBD (mutant) + RAP1A 
**[[1gua]] – hc-Raf RBD + RAP1A + GPPNHP 
**[[8jnb]] – hc-Raf RBD + ligand 
**[[4g0n]], [[4g3x]] – hc-Raf RBD + GTPase Hras 
**[[3kud]] – hc-Raf RBD (mutant) + GTPase Hras 
**[[8epw]], [[8t74]] – hc-Raf RBD + GTPase K-ras 
**[[8t75]], [[9ygs]] – hc-Raf RBD-CRD + GTPase K-ras + GMPPNP 
**[[9ay7]], [[9aya]] – hc-Raf + MEK1 
**[[9mmq]] – hc-Raf + MEK1 – Cryo EM 
**[[9mms]] – hc-Raf (mutant) + MEK1 – Cryo EM 
**[[9o0u]], [[9o0v]] – hc-Raf (mutant) + MEK1 + ANP + inhibitor– Cryo EM 
**[[8u1l]] – hc-Raf + Hsp90 + CDC37 – Cryo EM 
**[[8gae]], [[8gft]] – hc-Raf + Hsp90 + CDC37 + PP5 – Cryo EM 

*'''Snf1-related Chk'''

**[[3uc4]], [[3uc3]], [[3udb]], [[3zut]], [[3zuu]] – AtChk Srk2E kinase domain (mutant) – ''Arabidopsis thaliana'' 
**[[3ujg]] – AtChk Srk2E kinase domain (mutant) + protein phosphatase 2C 
**[[5yks]] – hChk 

*'''MAPK-interacting Chk''' or Mnk1 Mnk2

**[[2hw6]] – hMnk 1 catalytic domain 
**[[2hw7]] – hMnk 1 catalytic domain + staurosporin 
**[[5wvd]] – hMnk 1 catalytic domain + inhibitor 
**[[2ac3]] – hMnk 2 catalytic domain 
**[[2ac5]] – hMnk 2 catalytic domain (mutant) 
**[[6cj5]], [[6cje]], [[6cjh]], [[6cjw]], [[6cjy]], [[6ck3]], [[6ck6]], [[6cki]] – hMnk 2 catalytic domain (mutant) + inhibitor 

*'''hChk Pak''' or '''Chk N''' or '''PRK1'''; Domains - CRIB 74-109; Hr1B 122-199; catalytic 109-426; kinase 605-942

**[[1urf]] – hChk Pak-1 Hr1b domain - NMR 
**[[4nkg]] – hChk Pak-1 Hr1b domain + SSPH1 LRR domain 
**[[2rmk]] – hChk Pak-1 Hr1bb domain + Rac1 - NMR 
**[[1f3m]] – hChk Pak-1 autoregulatory+kinase domains 
**[[4otd]] - hChk Pak-1 kinase domain 
**[[1yhv]], [[1yhw]], [[3q4z]], [[3q52]], [[3q53]] – hChk Pak-1 kinase domain (mutant) 
**[[4o0r]], [[4o0t]], [[4zji]], [[4zjj]], [[4zlo]], [[4zy4]], [[4zy5]], [[4zy7]], [[5ime]], [[5kbq]], [[5kbr]], [[6b16]], [[7vto]] – hChk Pak-1 kinase domain + inhibitor 
**[[4oti]], [[4oth]], [[4otg]] – hChk Pak-1 kinase domain + inhibitor 
**[[4eqc]], [[4p90]], [[5dew]], [[5dey]], [[5dfp]] – hChk Pak-1 kinase domain (mutant) + inhibitor 
**[[2hy8]] – hChk Pak-1 kinase domain + staurosporin 
**[[2qme]] – hChk Pak-1 CRIB domain + RAC3 
**[[3fxz]], [[3fy0]], [[4daw]] – hChk Pak-1 kinase domain (mutant) + Ru complex 
**[[6fd3]] – hChk Pak-3 kinase domain (mutant) 
**[[2j0i]], [[4fie]] – hChk Pak-4 
**[[4fig]], [[4fij]], [[4l67]] – hChk Pak-4 kinase domain 
**[[2cdz]] – hChk Pak-4 + purine derivative 
**[[2ov2]] – hChk Pak-4 CRIB domain + RAC3 
**[[2qon]], [[4fif]], [[4fih]], [[4fii]], [[4jdh]], [[4jdi]], [[4jdj]], [[4jdk]], [[6wlx]], [[6wly]] – hChk Pak-4 kinase domain + peptide 
**[[4app]], [[4o0v]], [[4o0x]], [[4o0y]], [[4njd]], [[4xbu]], [[5bms]], [[5i0b]], [[5vee]], [[5vef]], [[5zjw]], [[5xvg]], [[5xvf]], [[5xva]], [[7cmb]], [[7cp3]], [[7cp4]] – hChk Pak-4 kinase domain + inhibitor 
**[[2x4z]], [[2xh5]] – hChk Pak-4 kinase domain (mutant) + inhibitor 
**[[5upl]], [[5upk]] – hChk Pak-4 kinase domain (mutant) + CDC42 
**[[5ved]] – hChk Pak-4 kinase domain + staurosporine 
**[[8ahi]] – hChk Pak-4 300-591 + inhibitor 
**[[7s46]], [[7s48]] – hChk Pak-4 catalytic domain + integrin beta-5 peptide 
**[[2c30]] – hChk Pak-6 
**[[2odb]] – hChk Pak-6 CRIB domain + CDC42 
**[[4ks8]] – hChk Pak-6 kinase domain + sunitinib 
**[[4ks7]] – hChk Pak-6 kinase domain (mutant) + inhibitor 
**[[2f57]] – hChk Pak-7 

*'''Mycobacterium tuberculosis Chk Pkn'''

**[[4x3f]] - MtChk PknA – ''Mycobacterium tuberculosis'' 
**[[4ow8]] - MtChk PknA kinase domain 
**[[3ori]], [[3ork]], [[3orl]], [[3orm]], [[3oro]], [[3orp]], [[3ort]] - MtChk PknB kinase domain (mutant) 
**[[1o6y]] – MtChk PknB kinase domain 
**[[6b2p]], [[6b2q]] – MtChk PknB kinase domain + inhibitor 
**[[2kud]], [[2kue]], [[2kuf]], [[2kui]] – MtChk PknB pasta domains 2-3 - NMR 
**[[3ouv]] – MtChk PknB pasta domain 3 
**[[5e0y]] – MtChk PknB pasta domain 4 
**[[5e10]] – MtChk PknB pasta domains 1-2 
**[[5e0z]] – MtChk PknB pasta domains 3-4 
**[[5e12]] – MtChk PknB pasta domains 2-4 
**[[5u94]] - MtChk PknB kinase domain + inhibitor 
**[[3f61]], [[3f69]] - MtChk PknB kinase domain (mutant) + inhibitor 
**[[6i2p]] - MtChk PknB kinase domain (mutant) + GARA + peptide 
**[[1rwi]], [[1rwl]] - MtChk PknD extracellular domain 
**[[2h34]] – MtChk PknE catalytic domain 
**[[7naa]] – MtChk PknF kinase domain + inhibitor 
**[[4y12]] - MtChk PknG + ATP-gS 
**[[4y0x]] - MtChk PknG + ADP 
**[[7q52]] - MtChk PknG + inhibitor 
**[[4esq]] - MtChk PknH extracellular domain 
**[[5m06]], [[5xka]] - MtChk PknI kinase domain 
**[[5m07]], [[5m08]], [[5m09]] - MtChk PknI kinase domain (mutant) 
**[[5xlm]], [[5xll]] - MtChk PknI sensor domain 
**[[7mxb]], [[7mxj]], [[7mxk]] - Chk PknG kinase domain + AMPPNP - Corynebacterium glutamicum 

*'''hChk Nek'''

**[[4apc]] – hChk Nek1 kinase domain (mutant) 
**[[4b9d]] - hChk Nek1 kinase domain (mutant) + inhibitor 
**[[2w5h]] – hChk Nek2 kinase domain 
**[[2jav]], [[2wqo]], [[2xk3]], [[2xk4]], [[2xk6]], [[2xk7]], [[2xk8]], [[2xkc]], [[2xkd]], [[2xke]], [[2xkf]], [[2xnm]], [[2xnn]], [[2xno]], [[2xnp]], [[4a4x]], [[4afe]], [[5m51]], [[5m53]], [[5m55]], [[5m57]], [[6sgd]], [[6sgh]], [[6sgi]], [[6sgk]], [[6sk9]] – hChk Nek2 + inhibitor 
**[[2w5a]], [[2w5b]] – hChk Nek2 + nucleotide 
**[[6tm5]] - hChk Nek2 in anaphase-promoting complex – Cryo EM 
**[[2wqm]], [[6s76]] – hChk Nek7 
**[[2wqn]] – hChk Nek7 + ADP 
**[[5de2]] – hChk Nek7 + hChk Nek9 
**[[6s73]], [[2wqo]] – hChk Nek7 + inhibitor 
**[[6npy]] – hChk Nek7 + Nlrp3 
**[[6s75]] – hChk Nek7 + inhibitor 

*'''Chk Rio'''

**[[6fdo]], [[6fdn]], [[6fdm]] – hChk Rio2 
**[[4otp]] – hChk Rio1 Rio domain + ADP 
**[[6hk6]], [[7vbt]] – hChk Rio2 + inhibitor 
**[[6eml]], [[6fai]], [[6g18]], [[6g51]], [[6rbd]],[[6rbe]], [[6y7c]] – yChk Rio2 in 40S particle – Cryo EM 
**[[1ztf]] – AfChk Rio1 + adenine derivative – Archaeoglobus fulgidus 
**[[1zth]] – AfChk Rio1 + ADP 
**[[1zp9]] – AfChk Rio1 + ATP 
**[[1tqp]], [[1zao]] – AfChk Rio2 + ATP 
**[[1zar]] – AfChk Rio2 + ADP 
**[[4gyg]] – CtChk Rio2 – Chaetonium thermophilum 
**[[4gyi]] – CtChk Rio2 + ADP 

*hChk Vrk (vaccinia-related kinase)

**[[2kty]], [[2kul]], [[2lav]], [[2rsv]] – hChk Vrk1 kinase domain 1-396 - NMR 
**[[3op5]] – hChk Vrk1 kinase domain (mutant) 
**[[5ukf]] – hChk Vrk1 kinase domain + inhibitor 
**[[5uvf]], [[6cnx]], [[6bu6]], [[6cfm]], [[6dd4]], [[6bp0]], [[6bru]], [[6btw]], [[6cmm]], [[6cqh]], [[6csw]], [[6npn]], [[6vxu]], [[6vzh]] – hChk Vrk1 kinase domain (mutant) + inhibitor 
**[[6ac9]] – hChk Vrk1 kinase domain (mutant) + AMPPNP 
**[[7tan]] – hChk Vrk1 kinase domain + nucleosome – Cryo EM 
**[[2v62]] – hChk Vrk2 kinase domain 
**[[5uu1]], [[6ncg]], [[8q1z]] – hChk Vrk2 kinase domain + inhibitor 

*Chk Wnk (protein kinase lysine-deficient); Domains - kinase 194-483; CCT1 454-549

**[[6cn9]], [[4q2a]], [[4pwn]] - hChk Wnk1 kinase domain (mutant) 
**[[5tf9]] - hChk Wnk1 kinase domain + inhibitor + AMPPNP 
**[[5wdy]], [[5we8]] - hChk Wnk1 kinase domain + inhibitor + ANP 
**[[5drb]], [[6ol2]]- rChk Wnk1 kinase domain (mutant) + inhibitor 
**[[6elm]] - hChk Wnk2 CCT1 domain 
**[[6fbk]] - hChk Wnk2 CCT1 domain + Wnk1 peptide 
**[[5o1v]], [[5o21]], [[5o23]] - hChk Wnk3 kinase domain 
**[[5o2c]] - hChk Wnk3 kinase + CCT1 domains 
**[[5o26]], [[5tf9]] - hChk Wnk3 kinase domain + AMPPNP 
**[[5o2b]] - hChk Wnk3 kinase domain + inhibitor 
**[[8edh]] - hChk Wnk3 kinase domain (mutant) + inhibitor 
**[[2lru]] – rChk Wnk1 autoinhibitory domain 480-572 - NMR 
**[[5w7t]] - rChk Wnk1 kinase domain 
**[[7uos]] - rChk Wnk1 kinase domain (mutant) 

*'''TANK-binding kinase'''

**[[4efo]] – hChk Tbk1 ubiquitin-like domain 
**[[6rsr]], [[6rsu]] – hChk Tbk1 + inhibitor 
**[[4im0]], [[4im2]], [[4im3]], [[4iw0]], [[4iwo]], [[4iwp]], [[4ipq]], [[6rst]] – hChk Tbk1 (mutant) + inhibitor 
**[[6cq5]], [[6cq4]], [[6cq0]], [[6boe]], [[6bod]], [[6bny]], [[5w5v]] – hChk Tbk1 + ulcer drug 
**[[4eut]], [[4euu]] – hChk Tbk1 kinase+ubiquitin-like domains (mutant) + inhibitor 
**[[6nt9]] – hChk Tbk1 (mutant) + STING 
**[[5eoa]], [[5eof]] – hChk Tbk1 residues 677-729 + optineurin 
**[[4jl9]], [[4jlc]] – mChk Tbk1 + inhibitor 
**[[6o8c]], [[6o8b]] – mChk Tbk1 (mutant) + STING 

*'''Haspin'''

**[[2vuw]], [[2wb8]] – hChk Haspin kinase domain 
**[[3dle]] – hChk Haspin kinase domain + AMP 
**[[3e7v]], [[3f2n]], [[3fmd]], [[3iq7]], [[4qtc]], [[5htb]], [[5htc]], [[6z56]], [[6z57]], [[6z58]], [[6z59]], [[6z5a]], [[6z5b]], [[6z5c]]. [[6z5d]], [[6z5e]] , [[7avq]], [[7ops]] – hChk Haspin kinase domain + inhibitor 
**[[7sqm]] – hChk Haspin kinase domain + antimalarial 
**[[6g38]], [[6g34]], [[6g35]], [[6g36]], [[6g37]] – hChk Haspin kinase domain + tubercidin derivative 
**[[6g39]], [[6g3a]] – hChk Haspin kinase domain (mutant) + tubercidin derivative 
**[[4ouc]] – hChk Haspin kinase domain + histone H3 peptide 

*'''MAP/microtubule affinity-regulating kinase (MARK)'''

**[[2hak]] – hChk MARK1 catalytic+UBA domains 
**[[3ose]] - hChk MARK1 KA1 domain 
**[[6c9d]] – hChk MARK1 catalytic+UBA+KA1 domains (mutant) 
**[[5eak]], [[5kz7]], [[5kz8]] – hChk MARK2 catalytic+UBA domains + inhibitor 
**[[3iec]] – hChk MARK2 catalytic+UBA domains + cytotoxicity-associated immunodominant antigen peptide 
**[[2qnj]] – hChk MARK3 catalytic+UBA domains 
**[[3fe3]] – hChk MARK3 catalytic+UBA domains (mutant) 
**[[7p1l]] – hChk MARK3 catalytic+UBA domains + inhibitor 
**[[5es1]] – hChk MARK4 catalytic+UBA domains + inhibitor 
**[[1zmu]] – rChk MARK2 catalytic+UBA domains 
**[[2wzj]], [[2r0i]], [[1zmv]], [[1y8g]], [[1zmw]] – rChk MARK2 catalytic+UBA domains (mutant) 
**[[1ul7]], [[1v5s]] - mChk MARK3 catalytic domain - NMR 

*'''Mitotic checkpoint Chk (Bub)'''; Domains: TPR 1-220; kinase 726-1085

**[[2lah]] – hChk Bub1 TPR domain – NMR 
**[[2wvi]] – hChk Bub1β TPR domain 
**[[3si5]] – hChk Bub1 TPR domain + CASC5 peptide 
**[[4r8q]], [[4qpm]], [[5dmz]] – hChk Bub1 kinase domain + ADP 
**[[6f7b]] – hChk Bub1 kinase domain + inhibitor 
**[[4a1g]] – hChk Bub1 TPR domain + CASC5 KI motif 
**[[4ggd]] - hChk Bub1 + cell division cycle protein 
**[[6tlj]], [[5khu]] - hChk Bub1 in anaphase-promoting complex – Cryo EM 
**[[6jkk]] – DmChk Bub1 kinase domain 
**[[6jkm]] – DmChk Bub1 kinase domain + ADP 
**[[5jja]] – hChk Bub1 residues 661-734 + PP2A 
**[[3esl]] – yChk Bub1 N terminal 
**[[4bl0]] - yChk Bub1 + cell cycle arrest protein Bub3 

*'''Microtubule-associated Chk'''

**[[2m9x]] – hChk 1 residues 187-287 – NMR 
**[[3ps4]] - hChk 1 residues 965-1057 
**[[2kqf]], [[2kyl]] – hChk 2 PDZ domain + glycoprotein C terminal – NMR 
**[[3khf]] - hChk 3 PDZ domain 
**[[2w7r]] – hChk 4 PDZ domain 

*'''mTOR''' or '''Mechanistic target of rapamycin'''

*''mTOR FRB domain residues 2015-2114''

**[[1nsg]], [[1fap]] – hFRAP FRB domain + FKBP 
**[[2rse]] – hFRAP FRB domain + FKBP – NMR 
**[[1aue]] – hFRAP FRB domain 
**[[2gaq]], [[2npu]] – hFRAP FRB domain - NMR 
**[[8ppz]] – hFRAP FRB domain + FKBP + pyridine derivative 
**[[3fap]], [[2fap]], [[4fap]] – hFRAP FRB domain + FKBP + rapamycin analog 
**[[4drh]], [[4dri]], [[4drj]], [[5gpg]] – hFRAP FRB domain + FKBP + rapamycin 
**[[6m4u]], [[6m4w]] – hChk Mtor FRB domain (mutant) + FKBP1A + rapamycin 
**[[5wbh]] – hFRAP FRB domain + S6K1 peptide 

*''mTOR FAT+PIKK domain residues 1376-2549''

**[[4jsn]] – hFRAP + TORC subunit LST8 
**[[4jsp]] – hFRAP + TORC subunit LST8 + ATP 
**[[4jsv]] – hFRAP + TORC subunit LST8 + ADP 
**[[4jsx]] – hFRAP + TORC subunit LST8 + torin2 
**[[4jt5]] – hFRAP + TORC subunit LST8 + pp242 
**[[4jt6]] – hFRAP + TORC subunit LST8 + PI-103 
**[[5wby]], [[5wbu]] – hFRAP + TORC subunit LST8 + proline-rich Akt1 substrate 

*''mTOR complex''

**[[5flc]] – hmTOR + RAPTOR + LST8 + FKBP – Cryo EM 
**[[5h64]] – hmTOR + RAPTOR + LST8 – Cryo EM 
**[[6sb2]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC – Cryo EM 
**[[6sb0]] – hChk Mtor + RAPTOR + LST8 + RAGA + RAGC + proline-rich Akt1 substrate – Cryo EM 
**[[5zcs]] – hmTOR + LST8 + AVO3 + TORC2 – Cryo EM 
**[[7tzo]] – hTORC2 in mTORC2 complex– Cryo EM 
**[[6zwm]], [[6zwo]], [[7owg]], [[7pe7]], [[7pe8]], [[7pe9]], [[7pea]], [[7peb]], [[7pec]], [[7uxc]] , [[8era]]– mTOR in mTor complex – Cryo EM 

*'''Gcn2'''

**[[1zyc]] – yChk Gcn2 
**[[1zxe]], [[1zy4]], [[1zy5]] – yChk Gcn2 (mutant) 
**[[2yz0]] – yChk Gcn2 RWD/GI domain – NMR 
**[[4otm]] – yChk Gcn2 C terminal domain 
**[[1zyd]] – yChk Gcn2 + ATP 
**[[4otn]] – mChk Gcn2 C terminal domain 

*'''LRRK1''' or leucine-rich repeat Chk1

**[[8e04]], [[8e05]], [[8e06]], [[8fac]] – hLRRK1 – Cryo EM 

*'''LRRK2''' or leucine-rich repeat Chk2 or dardarin

**[[6xr4]] – hLRRK2 – Cryo EM 
**[[7lht]], [[7lhw]], [[7li4]] – hLRRK2 + ATP + GDP – Cryo EM 
**[[7li3]] – hLRRK2 (mutant) + ATP + GDP – Cryo EM 
**[[6oje]], [[7thy]] – hLRRK2 GTPase domain 1329-1520 
**[[6ojf]] – hLRRK2 GTPase domain (mutant) 
**[[6dlo]], [[6dlp]] – hLRRK2 WD40 domain 
**[[7thz]] – hLRRK2 1330-1527 + GDP 
**[[6vno]], [[6vp6]], [[6vp7]] – hLRRK2 C terminal 1330-2527 – Cryo EM 
**[[6vp8]] – hLRRK2 C terminal 1330-2527 + COR domain 1670-1950 + WD40 domain 2140-2489 – Cryo EM 
**[[6s6q]] – AtLRRK2 ectodomain + protein casparian strip peptide 

*'''Pim'''

*Pim1 catalytic domain residues 14-313

**[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain 
**[[1yxs]] – hPim1 catalytic domain (mutant) 
**[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP 
**[[1yxu]] – hPim1 catalytic domain + AMP 
**[[1yxv]], [[5ipj]] – hPim1 catalytic domain + quinoline derivative 
**[[1yxx]] – hPim1 catalytic domain + indole derivative 
**[[2bzh]], [[2bzi]], [[2bzj]] – hPim1 catalytic domain (mutant) + organometallic ligand 
**[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3c4e]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umw]], [[3umx]], [[4enx]], [[4eny]], [[4k1b]], [[4k18]], [[4k0y]], [[4iaa]], [[4i41]], [[4ll5]], [[4lm5]], [[4lmu]], [[4mta]], [[4med]], [[4mbl]], [[4mbi]], [[4n6y]], [[4n6z]], [[4n70]], [[4xh6]], [[5iis]], [[5kgd]], [[5kge]], [[5kgg]], [[5kgi]], [[5kgk]], [[5kzi]], [[5vua]], [[5vub]], [[5vuc]], [[6mt0]], [[6vrv]], [[7oov]], [[7oow]], [[7oox]], [[7xsv]] – hPim1 catalytic domain + inhibitor 
**[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor 

*Pim1 kinase domain residues 92-404

**[[4jx3]] – hPim1 kinase domain 
**[[3uix]], [[5c1q]] – hPim1 kinase domain residues 120-404 + quinoline derivative 
**[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate 
**[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand 
**[[1xws]], [[4alu]], [[4alv]], [[4alw]], [[4as0]], [[4bzn]], [[4bzo]], [[4dtk]], [[4jx7]], [[4rbl]], [[4rc2]], [[4rc3]], [[4rc4]], [[4ty1]], [[4wrs]], [[4wsy]], [[4wt6]], [[4xhk]], [[5dgz]], [[5dhj]], [[5dia]], [[5dwr]], [[5eol]], [[5kcx]], [[5o11]], [[5o12]], [[5o13]], [[5tel]], [[5tex]], [[5toe]], [[5v80]], [[5v82]]. [[6bsk]], [[6kzi]], [[6l11]], [[6l12]], [[6l13]], [[6l14]], [[6l15]], [[6l16]], [[6l17]], [[6no8]], [[6no9]], [[6vru]], [[6ykd]], [[7zun]] – hPim1 kinase domain + inhibitor 
**[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor 

*Pim1 full length

**[[4rpv]], [[5tur]] - hPim1 + inhibitor 

*Pim1 complex with consensus peptide (pimtide)

**[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6qxk]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]] – hPim1 kinase domain + inhibitor + consensus peptide 
**[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide 
**[[2c3i]], [[5ndt]], [[5n5m]], [[5n5l]], [[5n52]], [[5n51]], [[5n50]], [[5n4z]], [[5n4y]], [[5n4x]], [[5n4v]], [[5n4u]], [[5n4r]], [[5n4o]], [[5n4n]], [[5mzl]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide 
**[[4gw8]], [[7qb2]], [[7qfm]], [[7z6u]], [[8afr]] – hPim1 catalytic domain (mutant) + inhibitor + pimtide 
**[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide 
**[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide 

*Pim1 containing phosphorylated Ser 261

**[[1yhs]] – hPim1 kinase domain + PSer + staurosporine 
**[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor 
**[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor 
**[[1yi4]] – hPim1 kinase domain + PSer + adenosine 

*Pim2

**[[4x7q]] – hPim2 catalytic domain + inhibitor 
**[[2iwi]] – hPim2 catalytic domain + Ru ligand 

*'''Rip or receptor-interacting Chk; Domains – catalytic 1-294; Amyloid fibril 418-518; Death 561-671'''

**[[6ac5]] – hRip1 death domain 
**[[6r5f]], [[6nw2]], [[6c4d]], [[6c3e]], [[5tx5]], [[7fcz]], [[7fd0]], [[7ydx]] – hRip1 catalytic domain + inhibitor 
**[[6rln]], [[6ocq]], [[6nyh]], [[6hho]] – hRip1 catalytic domain (mutant) + inhibitor 
**[[6ggs]] – hRip2 – Cryo EM 
**[[5yrn]] – hRip2 CARD domain 434-540 – Cryo EM 
**[[6szj]], [[6sze]], [[6s1f]], [[6rna]], [[6rn8]], [[6hmx]], [[6fu5]], [[6es0]], [[5w5o]], [[5w5j]] – hRip2 catalytic domain + inhibitor 
**[[6ul8]] – hRip2 catalytic domain (mutant) + inhibitor 
**[[8aza]] – hRip2 catalytic domain + XiaP Bir2 domain – Cryo EM 
**[[7mx3]] – hRip3 catalytic domain (mutant) + inhibitor 
**[[7mon]] – hRip3 catalytic domain (mutant) + MLKL 
**[[7dac]] – hRip3 amyloid fibril - NMR 
**[[7da4]] – hRip3 amyloid fibril – Cryo EM 
**[[6oko]] – mRip3 catalytic domain + inhibitor 
**[[6jpd]] – mRip3 residues 409-486 - NMR 
**[[5wnm]], [[5wnj]] – mRip4 catalytic domain (mutant) + drug 
**[[5wnl]] – mRip4 catalytic domain (mutant) + staurosporine 
**[[5wnk]] – mRip4 catalytic domain (mutant) + inhibitor 
**[[5wni]] – mRip4 catalytic domain (mutant) + ATP 
**[[6gwm]] – rRip2 caspase recruitment domain 433-539 

*'''Ulk'''

**[[6qas]] – hChk Ulk1 + inhibitor 
**[[5ci7]], [[6mnh]] – hChk Ulk1 (mutant) + inhibitor 
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog 
**[[8soi]], [[8sqz]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein 
**[[8srm]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein – Cryo EM 
**[[8srq]] – hChk Ulk1 + RB1-inducible coiled-coil protein + autophagy-related protein + PI3K – Cryo EM 
**[[6qav]], [[6qau]], [[6qat]], [[6yid]] – hChk Ulk2 + inhibitor 
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor 
**[[6fdz]], [[6fdy]] – hChk Ulk3 + leukemia drug 
**[[6tsz]] – hChk Ulk4 pseudfokinase domain + ATPgS 
**[[6u5l]] – hChk Ulk4 (mutant) + inhibitor 

*'''Hipa''' and '''Hipb'''

**[[3tpd]], [[3tpe]] – EcChk Hipa – ''Escherichia coli'' 
**[[3tpb]], [[3dnt]], [[3dnu]] – EcChk Hipa (mutant) 
**[[4pu7]], [[4pu8]] – SoChk Hipb - ''Shewanella oneidensis'' 
**[[3tpt]] – EcChk Hipa (mutant) + ADP 
**[[3fbr]] – EcChk Hipa (mutant) + AMPPNP + peptide 
**[[3tpv]] – EcChk Hipa + ADP 
**[[2wiu]] – EcChk Hipa + Hipb 
**[[4yg7]], [[5k98]], [[3hzi]], [[3dnv]] – EcChk Hipa + Hipb + DNA 
**[[4yg1]], [[4z58]], [[4z59]], [[4z5c]], [[4z5d]] – EcChk Hipb + DNA 
**[[4z5h]] – EcChk Hipb (mutant) + DNA 
**[[4pu3]], [[4pu4]] – SoChk Hipa + Hipb + DNA - ''Shewanella oneidensis'' 
**[[4pu5]] – SoChk Hipa + AMPPNP 

*'''Chk Smg'''

**[[6l53]] – hChk Smg1 – Cryo EM 
**[[7pw6]] – hChk Smg1 + inhibitor – Cryo EM 
**[[7pw7]] – hChk Smg1 + Smg9 + inhibitor – Cryo EM 
**[[7pw9]] – hChk Smg1 + Smg9 + AMPPNP + ATP – Cryo EM 
**[[6l54]], [[6syt]] – hChk Smg1 + Smg8 + Smg9 – Cryo EM 
**[[7pw4]], [[7pw5]] – hChk Smg1 + Smg8 + Smg9 + inhibitor – Cryo EM 
**[[7pw8]] – hChk Smg1 + Smg8 + Smg9 + AMPPNP – Cryo EM 
**[[6z3r]] – hChk Smg1 + Smg8 + Smg9 + regulator of nonsense transcripts – Cryo EM 
**[[2hwy]] – hChk Smg5 PIN domain 
**[[2hww]], [[2hwx]] – hChk Smg6 PIN domain (mutant) 
**[[4um2]] – hChk Smg6 TPR domain 
**[[1ya0]] – hChk Smg7 N terminal 

*'''Chk Vprbp or DCAF1'''

**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain 1039-1401 (mutant) 
**[[7sse]], [[7ufv]], [[8f8e]], [[8og5]], [[8og6]], [[8og7]], [[8og8]], [[8og9]], [[8oga]], [[8ogb]], [[8ogc]], [[8oo5]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) + inhibitor 
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM 
**[[5aja]] – hChk Vprbp WD repeat domain + VPX + SAMHD1 

*'''Other Chk'''

**[[1wak]] – hChk Sprk1 
**[[3dak]] – hChk Osr1 kinase domain 
**[[7okw]] – hChk Osr1 C-terminal 
**[[4aw2]] – hChk Mrckα kinase domain 
**[[4pxw]], [[8ood]] – hChk Vprbp WD repeat domain (mutant) 
**[[7v7c]] – hChk Vprbp in DDB1-VPRBP-VPR-UNG2 complex – Cryo EM 
**[[1uf0]] – hChk Dcamkl1 DCX domain – NMR 
**[[1u5q]] – rChk Tao2 kinase domain 
**[[2cos]] – mChk Lats2 – NMR 
**[[1xte]], [[1xtn]], [[6edx]] – mChk Sgk3 PX domain 
**[[4yom]] – mChk Brsk2 
**[[4ynz]] – mChk Brsk1 N terminal domain 
**[[5iri]] – mChk Brsk1 residues 592-719 
**[[5oat]], [[7mp8]] – rfbChk Pink1– red flour beetle 
**[[7t3x]] – Chk Pink1 (mutant) – louse 
**[[4f0g]] – smChk Roco4 kinase domain – slime mold 
**[[5tos]] – AtChk Bik1 
**[[1q8z]], [[1zyc]] – yChk 
**[[1how]], [[1zxe]], [[1zy4]] – yChk (mutant) 
**[[1ow5]], [[1x9x]] – yChk Ste11 SAM domain – NMR 
**[[2kio]], [[2kit]], [[1w1n]] – yChk Tor1 FATC domain – NMR 
**[[3gre]] – yChk Vps15 WD repeat domain 
**[[3osm]], [[3ost]] - yChk Kcc4 kinase domain 
**[[5yyx]] – yChk Mek1 FHA domain 
**[[6jxc]], [[6jxa]] – yChk Tel1 – Cryo EM 
**[[6u69]] – CaChk Yck2 – ''Candida albicans'' 
**[[6sl1]], [[6sl0]], [[6skz]], [[6sky]] – Chk Tel1 – ''Chaetonium thermophilum'' – Cryo EM 
**[[6ra0]] – CeChk Dkf1 – ''Chaenorhabditis elegans'' 
**[[7z6e]] – CeChk Mrck1 regulatory domain 
**[[6tlb]] – Chk – ''Plasmodium falciparum'' 

*Other Chk complexes

**[[1wbp]], [[7dd1]] – hChk Sprk1 + peptide 
**[[3beg]] – hChk Srpk1 + splicing factor SF2 
**[[3hdm]], [[3hdn]], [[7pue]] – hChk Sgk1 (mutant) + inhibitor 
**[[2r5t]] – hChk Sgk3 + AMPPNP 
**[[4yff]], [[4yfi]], [[6b5j]], [[7mgj]], [[7mgk]] – hChk Tnni3k + inhibitor 
**[[2v3s]] – hChk Osr1 + hChk Wnk4 peptide 
**[[2vwi]] – hChk Osr1 kinase domain + ANP 
**[[7que]], [[7quf]] – hChk Drak1 kinase domain + inhibitor 
**[[4crs]] – hChk N2 kinase domain + ATPγS 
**[[3tku]], [[4ual]], [[3qfv]], [[5ote]], [[5otf]] – hChk Mrckβ + inhibitor 
**[[4uak]] – hChk Mrckβ + ADP 
**[[5aja]], [[4z8l]], [[4cc9]] – hChk Vprbp WD repeat domain + VPX + SAMHD1 
**[[5jk7]] – hChk Vprbp WD repeat domain + VPX + DDB1 + UDG 
**[[3wa0]], [[4p7i]] – hChk Vprbp residues 1417-1506 + merlin 
**[[4wzx]] – hChk Ulk3 MIT 2 domain + inhibitor 
**[[5ci7]] – hChk Ulk1 (mutant) + inhibitor 
**[[4wnp]], [[4wno]] – hChk Ulk1 + IST1 homolog 
**[[5b5w]], [[5b6b]], [[5brk]] – hChk Lats1 residues 622-704 + MOB1 
**[[5yz0]] – hChk Atr + Atr-interacting protein – Cryo EM 
**[[6bdn]] – hChk Tao3 kinase domain + ADP 
**[[5yh3]] – hChk Fam20C 141-578 + pseudokinase Fam20A 
**[[2gcd]] – rChk Tao2 kinase domain + staurosporine 
**[[1u5r]] – rChk Tao2 kinase domain + ATP 
**[[5yj9]], [[7mp9]] – rfbChk Pink1 kinase domain + AMPPNP 
**[[6bn1]] – DmChk Hippo SARAH domain + Shar-Pei 
**[[3hgk]] – Chk Pto + effector protein AVRPTOB – Currant tomato 
**[[3p86]], [[3ppz]] - AtChk Ctr1 + staurosporine 
**[[4f0f]] – smChk Roco4 kinase domain + APPCP 
**[[4f1m]], [[4f1o]] – smChk Roco4 kinase domain (mutant) + APPCP 
**[[4f1t]], [[4yzm]], [[4yzn]] – smChk Roco4 kinase domain + inhibitor 
**[[5fvm]] - Tor2 + LST8 - ''Kluyveromyces marxianus'' 
**[[5kc2]] - yVps15 + Vps34 - Cryo EM 
**[[5dfz]] - yVps15 + Vps34 + Vps30 + VPSAP28 + VPSAP30 - Cryo EM 
**[[1q8y]], [[1q97]], [[1q99]], [[1zyd]] – yChk + nucleotide 
**[[1zy5]] – yChk (mutant) + nucleotide 
**[[2jd5]] – yChk + NPL-3P 
**[[4lqs]], [[4lqq]], [[4lqp]] – yChk Cbk1 residues 251-756 + Cbk1 activator Mob2 
**[[6emk]] – yChk Tor2 + LST8 + TSC11 + AVO1 + AVO2 – Cryo EM 
**[[6s8f]] – yChk Tel1 + AMPPNP – Cryo EM 
**[[5yyz]] – yChk Mek1 FHA domain + Hop1 
**[[5x6o]], [[6z3a]], [[7wzr]], [[7wzw]]– yChk Mec1 + LCD1 – Cryo EM 
**[[6z2w]], [[6z2x]] – yChk Mec1 (mutant) + LCD1 – Cryo EM 
**[[7kue]] – yChk Kin28 in TFIIK complex – Cryo EM 
**[[6u6a]] – CaChk Yck2 + inhibitor 
**[[5fvm]] – Chk Tor2 + LST8 – ''Kluyveromyces maximanus'' 

*Serine/threonine protein kinase Rad53 see [[Rad53]]

*Serine/threonine protein kinase Gsk3B see [[Glycogen synthase kinase 3]]

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[[Category:Topic Page]]