3b25

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==Hsp90 alpha N-terminal domain in complex with an inhibitor CH4675194==
==Hsp90 alpha N-terminal domain in complex with an inhibitor CH4675194==
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<StructureSection load='3b25' size='340' side='right' caption='[[3b25]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<StructureSection load='3b25' size='340' side='right'caption='[[3b25]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3b25]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B25 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B25 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3b25]] is a 1 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=3B25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B25 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2K:4-METHYL-6-(TOLUENE-4-SULFONYL)-PYRIMIDIN-2-YLAMINE'>B2K</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B2K:4-METHYL-6-(TOLUENE-4-SULFONYL)-PYRIMIDIN-2-YLAMINE'>B2K</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b24|3b24]], [[3b26|3b26]], [[3b27|3b27]], [[3b28|3b28]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3b24|3b24]], [[3b26|3b26]], [[3b27|3b27]], [[3b28|3b28]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b25 OCA], [http://pdbe.org/3b25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3b25 RCSB], [http://www.ebi.ac.uk/pdbsum/3b25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3b25 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b25 OCA], [https://pdbe.org/3b25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b25 RCSB], [https://www.ebi.ac.uk/pdbsum/3b25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b25 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[[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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Heat Shock Proteins|Heat Shock Proteins]]
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Fukami, T A]]
[[Category: Fukami, T A]]
[[Category: Ono, N]]
[[Category: Ono, N]]
[[Category: Chaperone-chaperone inhibitor complex]]
[[Category: Chaperone-chaperone inhibitor complex]]

Revision as of 11:21, 5 January 2022

Hsp90 alpha N-terminal domain in complex with an inhibitor CH4675194

PDB ID 3b25

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