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==Human Heat Shock Protein 90 bound to 6-Hydroxy-3-(3-methyl-benzyl)-1H-indazole-5-carboxylic acid methyl-(4-morpholin-4-yl-phenyl)-amide==
==Human Heat Shock Protein 90 bound to 6-Hydroxy-3-(3-methyl-benzyl)-1H-indazole-5-carboxylic acid methyl-(4-morpholin-4-yl-phenyl)-amide==
<StructureSection load='5oci' size='340' side='right' caption='[[5oci]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
<StructureSection load='5oci' size='340' side='right'caption='[[5oci]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5oci]] 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=5OCI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OCI FirstGlance]. <br>
<table><tr><td colspan='2'>[[5oci]] 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=5OCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OCI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9R8:6-Hydroxy-3-(3-methyl-benzyl)-1H-indazole-5-carboxylic+acid+methyl-(4-morpholin-4-yl-phenyl)-amide'>9R8</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]] 1.62&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9R8:6-Hydroxy-3-(3-methyl-benzyl)-1H-indazole-5-carboxylic+acid+methyl-(4-morpholin-4-yl-phenyl)-amide'>9R8</scene></td></tr>
<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=5oci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oci OCA], [http://pdbe.org/5oci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oci RCSB], [http://www.ebi.ac.uk/pdbsum/5oci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oci 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=5oci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oci OCA], [https://pdbe.org/5oci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oci RCSB], [https://www.ebi.ac.uk/pdbsum/5oci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oci ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>
[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 5oci" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5oci" style="background-color:#fffaf0;"></div>
==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Amaral, M]]
[[Category: Large Structures]]
[[Category: Ecker, G F]]
[[Category: Amaral M]]
[[Category: Frech, M]]
[[Category: Ecker GF]]
[[Category: Graedler, U]]
[[Category: Frech M]]
[[Category: Grandits, M]]
[[Category: Graedler U]]
[[Category: Musil, D]]
[[Category: Grandits M]]
[[Category: Richter, L]]
[[Category: Musil D]]
[[Category: Schuetz, D A]]
[[Category: Richter L]]
[[Category: Atp-binding]]
[[Category: Schuetz DA]]
[[Category: Atpase]]
[[Category: Chaperone]]
[[Category: Heat shock]]
[[Category: Heat-shock protein complex]]
[[Category: Hsp90]]
[[Category: Nucleotide-binding]]
[[Category: Phosphorylation]]
[[Category: Pyrazole]]
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