3ekr: Difference between revisions

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<StructureSection load='3ekr' size='340' side='right'caption='[[3ekr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3ekr' size='340' side='right'caption='[[3ekr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ekr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EKR FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ekr]] 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=3EKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EKR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PY9:4-{[(2R)-2-(2-METHYLPHENYL)PYRROLIDIN-1-YL]CARBONYL}BENZENE-1,3-DIOL'>PY9</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3eko|3eko]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PY9:4-{[(2R)-2-(2-METHYLPHENYL)PYRROLIDIN-1-YL]CARBONYL}BENZENE-1,3-DIOL'>PY9</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3ekr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ekr OCA], [https://pdbe.org/3ekr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ekr RCSB], [https://www.ebi.ac.uk/pdbsum/3ekr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ekr ProSAT]</span></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=3ekr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ekr OCA], [https://pdbe.org/3ekr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ekr RCSB], [https://www.ebi.ac.uk/pdbsum/3ekr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ekr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gajiwala, K S]]
[[Category: Gajiwala KS]]
[[Category: Alternative splicing]]
[[Category: Atp-binding]]
[[Category: Chaperone]]
[[Category: Cytoplasm]]
[[Category: Hsp90 inhibitor]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: Stress response]]

Latest revision as of 13:08, 30 August 2023

Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone

3ekr, resolution 2.00Å

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