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7lsz

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<StructureSection load='7lsz' size='340' side='right'caption='[[7lsz]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='7lsz' size='340' side='right'caption='[[7lsz]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7lsz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LSZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7lsz]] 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=7LSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LSZ FirstGlance]. <br>
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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=ONG:{3-[(2,3-dihydro-1,4-benzodioxin-6-yl)sulfanyl]-4-hydroxyphenyl}(1,3-dihydro-2H-isoindol-2-yl)methanone'>ONG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-chaperonin_molecular_chaperone_ATPase Non-chaperonin molecular chaperone ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.10 3.6.4.10] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ONG:{3-[(2,3-dihydro-1,4-benzodioxin-6-yl)sulfanyl]-4-hydroxyphenyl}(1,3-dihydro-2H-isoindol-2-yl)methanone'>ONG</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=7lsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lsz OCA], [https://pdbe.org/7lsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lsz RCSB], [https://www.ebi.ac.uk/pdbsum/7lsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lsz 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=7lsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lsz OCA], [https://pdbe.org/7lsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lsz RCSB], [https://www.ebi.ac.uk/pdbsum/7lsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lsz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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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>
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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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</div>
</div>
<div class="pdbe-citations 7lsz" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 7lsz" style="background-color:#fffaf0;"></div>
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==See Also==
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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: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Non-chaperonin molecular chaperone ATPase]]
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[[Category: Balch M]]
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[[Category: Balch, M]]
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[[Category: Deng J]]
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[[Category: Deng, J]]
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[[Category: Matts R]]
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[[Category: Matts, R]]
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[[Category: Peng S]]
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[[Category: Peng, S]]
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[[Category: Chaperone]]
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[[Category: Hsp90a]]
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[[Category: Inhibitor]]
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Current revision

Hsp90a N-terminal inhibitor

PDB ID 7lsz

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