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4efu

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==Hsp90 Alpha N-terminal Domain in Complex with an Inhibitor 6-Hydroxy-3-(3-methyl-benzyl)-1H-indazole-5-carboxylic acid benzyl-methyl-amide==
==Hsp90 Alpha N-terminal Domain in Complex with an Inhibitor 6-Hydroxy-3-(3-methyl-benzyl)-1H-indazole-5-carboxylic acid benzyl-methyl-amide==
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<StructureSection load='4efu' size='340' side='right' caption='[[4efu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4efu' size='340' side='right'caption='[[4efu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4efu]] 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=4EFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EFU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4efu]] is a 1 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=4EFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EFU 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=EFU:N-BENZYL-6-HYDROXY-N-METHYL-3-(3-METHYLBENZYL)-1H-INDAZOLE-5-CARBOXAMIDE'>EFU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=EFU:N-BENZYL-6-HYDROXY-N-METHYL-3-(3-METHYLBENZYL)-1H-INDAZOLE-5-CARBOXAMIDE'>EFU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b28|3b28]], [[4eeh|4eeh]], [[4eft|4eft]]</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=4efu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efu OCA], [https://pdbe.org/4efu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4efu RCSB], [https://www.ebi.ac.uk/pdbsum/4efu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4efu ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90A ([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='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=4efu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efu OCA], [http://pdbe.org/4efu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4efu RCSB], [http://www.ebi.ac.uk/pdbsum/4efu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4efu ProSAT]</span></td></tr>
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</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/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Buchstaller, H P]]
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[[Category: Large Structures]]
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[[Category: Graedler, U]]
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[[Category: Buchstaller H-P]]
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[[Category: Lehmann, M]]
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[[Category: Graedler U]]
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[[Category: Musil, D]]
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[[Category: Lehmann M]]
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[[Category: Atp binding]]
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[[Category: Musil D]]
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[[Category: Chaperone-chaperone inhibitor complex]]
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Revision as of 07:09, 28 September 2022

Hsp90 Alpha N-terminal Domain in Complex with an Inhibitor 6-Hydroxy-3-(3-methyl-benzyl)-1H-indazole-5-carboxylic acid benzyl-methyl-amide

PDB ID 4efu

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