9cxm: Difference between revisions

Latest revision as of 06:36, 5 February 2025

Crystal structure of Human FN3K bound with ATP and DMF

Structural highlights

9cxm is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.76Å
Ligands:	A1A0O, ADP, ATP, EDO, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FN3K_HUMAN Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate (PubMed:11016445, PubMed:11522682, PubMed:11975663). Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions (PubMed:11522682, PubMed:11975663). Involved in intracellular deglycation in erythrocytes (PubMed:11975663). Involved in the response to oxidative stress by mediating deglycation of NFE2L2/NRF2, glycation impairing NFE2L2/NRF2 function (By similarity). Also able to phosphorylate psicosamines and ribulosamines (PubMed:14633848).[UniProtKB:Q9ER35]^[1] ^[2] ^[3] ^[4]

References

↑ Delpierre G, Rider MH, Collard F, Stroobant V, Vanstapel F, Santos H, Van Schaftingen E. Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. Diabetes. 2000 Oct;49(10):1627-34. PMID:11016445 doi:10.2337/diabetes.49.10.1627
↑ Szwergold BS, Howell S, Beisswenger PJ. Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo. Diabetes. 2001 Sep;50(9):2139-47. PMID:11522682 doi:10.2337/diabetes.50.9.2139
↑ Delpierre G, Collard F, Fortpied J, Van Schaftingen E. Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes. Biochem J. 2002 Aug 1;365(Pt 3):801-8. PMID:11975663 doi:10.1042/BJ20020325
↑ Collard F, Delpierre G, Stroobant V, Matthijs G, Van Schaftingen E. A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines. Diabetes. 2003 Dec;52(12):2888-95. PMID:14633848 doi:10.2337/diabetes.52.12.2888

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Delpierre G, Rider MH, Collard F, Stroobant V, Vanstapel F, Santos H, Van Schaftingen E. Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. Diabetes. 2000 Oct;49(10):1627-34. PMID:11016445 doi:10.2337/diabetes.49.10.1627

[2] Szwergold BS, Howell S, Beisswenger PJ. Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo. Diabetes. 2001 Sep;50(9):2139-47. PMID:11522682 doi:10.2337/diabetes.50.9.2139

[3] Delpierre G, Collard F, Fortpied J, Van Schaftingen E. Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes. Biochem J. 2002 Aug 1;365(Pt 3):801-8. PMID:11975663 doi:10.1042/BJ20020325

[4] Collard F, Delpierre G, Stroobant V, Matthijs G, Van Schaftingen E. A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines. Diabetes. 2003 Dec;52(12):2888-95. PMID:14633848 doi:10.2337/diabetes.52.12.2888

[1]

[2]

[3]

[4]

@@ Line 5: / Line 5: @@
 <table><tr><td colspan='2'>[[9cxm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CXM FirstGlance]. <br>
 </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
-<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1A0O:(3~{S},4~{R},5~{R})-1-morpholin-4-yl-3,4,5,6-tetrakis(oxidanyl)hexan-2-one'>A1A0O</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1A0O:1-deoxy-1-(morpholin-4-yl)-D-fructose'>A1A0O</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9cxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cxm OCA], [https://pdbe.org/9cxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cxm RCSB], [https://www.ebi.ac.uk/pdbsum/9cxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cxm ProSAT]</span></td></tr>
 </table>

9cxm: Difference between revisions

Latest revision as of 06:36, 5 February 2025

Crystal structure of Human FN3K bound with ATP and DMF

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools