6xlh
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS== | |
| + | <StructureSection load='6xlh' size='340' side='right'caption='[[6xlh]], [[Resolution|resolution]] 2.83Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6xlh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XLH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.83Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xlh OCA], [https://pdbe.org/6xlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xlh RCSB], [https://www.ebi.ac.uk/pdbsum/6xlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xlh ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HSC82_YEAST HSC82_YEAST] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity (By similarity). Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.<ref>PMID:11094077</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Agard DA]] | ||
| + | [[Category: Elnatan D]] | ||
| + | [[Category: Liu YX]] | ||
| + | [[Category: Myasnikov AG]] | ||
| + | [[Category: Sun M]] | ||
Current revision
Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS
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