6h4k
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structure of the Usp25 C-terminal domain== | |
- | + | <StructureSection load='6h4k' size='340' side='right'caption='[[6h4k]], [[Resolution|resolution]] 2.05Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6h4k]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H4K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H4K FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |
- | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6h4h|6h4h]]</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=6h4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h4k OCA], [http://pdbe.org/6h4k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h4k RCSB], [http://www.ebi.ac.uk/pdbsum/6h4k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h4k ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/UBP25_HUMAN UBP25_HUMAN]] Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains. The muscle-specific isoform (USP25m) may have a role in the regulation of muscular differentiation and function. | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Ubiquitinyl hydrolase 1]] | ||
+ | [[Category: Kisker, C]] | ||
+ | [[Category: Klemm, T A]] | ||
+ | [[Category: Sauer, F]] | ||
+ | [[Category: Cancer]] | ||
+ | [[Category: Deubiquitinase]] | ||
+ | [[Category: Immune system]] | ||
+ | [[Category: Ubiquitin]] | ||
+ | [[Category: Usp]] |
Revision as of 06:37, 27 March 2019
Structure of the Usp25 C-terminal domain
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