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1cmx

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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=1cmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cmx RCSB], [http://www.ebi.ac.uk/pdbsum/1cmx 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=1cmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cmx RCSB], [http://www.ebi.ac.uk/pdbsum/1cmx PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/UBL1_YEAST UBL1_YEAST]] Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or RUB1. Preferentially cleaves ubiquitin from peptides and small adducts.<ref>PMID:2555355</ref> <ref>PMID:12455997</ref> <ref>PMID:17709260</ref> <ref>PMID:21762696</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 04:54, 25 December 2014

STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES

1cmx, resolution 2.25Å

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