4gof

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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=4gof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gof OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gof RCSB], [http://www.ebi.ac.uk/pdbsum/4gof PDBsum]</span></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=4gof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gof OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gof RCSB], [http://www.ebi.ac.uk/pdbsum/4gof PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/SGTA_HUMAN SGTA_HUMAN]] Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity.<ref>PMID:18759457</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 11:03, 25 December 2014

Crystal structure of the SGTA homodimerization domain with covalent modifications to both C38

4gof, resolution 1.35Å

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