4yku
From Proteopedia
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==Heat Shock Protein 90 Bound to CS311== | ==Heat Shock Protein 90 Bound to CS311== | ||
| - | <StructureSection load='4yku' size='340' side='right' caption='[[4yku]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='4yku' size='340' side='right'caption='[[4yku]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4yku]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YKU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4yku]] 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=4YKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YKU FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4ER:6-(2-CHLOROPHENYL)-1,3,5-TRIAZINE-2,4-DIAMINE'>4ER</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4ER:6-(2-CHLOROPHENYL)-1,3,5-TRIAZINE-2,4-DIAMINE'>4ER</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ykq|4ykq]], [[4ykr|4ykr]], [[4ykt|4ykt]], [[4ykw|4ykw]], [[4ykx|4ykx]], [[4yky|4yky]], [[4ykz|4ykz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ykq|4ykq]], [[4ykr|4ykr]], [[4ykt|4ykt]], [[4ykw|4ykw]], [[4ykx|4ykx]], [[4yky|4yky]], [[4ykz|4ykz]]</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=4yku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yku OCA], [http://pdbe.org/4yku PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yku RCSB], [http://www.ebi.ac.uk/pdbsum/4yku PDBsum]</span></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='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=4yku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yku OCA], [http://pdbe.org/4yku PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yku RCSB], [http://www.ebi.ac.uk/pdbsum/4yku PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yku 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> | [[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> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Heat Shock Proteins|Heat Shock Proteins]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Kang, Y N]] | [[Category: Kang, Y N]] | ||
[[Category: Stuckey, J A]] | [[Category: Stuckey, J A]] | ||
Revision as of 06:49, 12 June 2019
Heat Shock Protein 90 Bound to CS311
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