5uhk
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of the core catalytic domain of Human O-GlcNAcase== | |
- | + | <StructureSection load='5uhk' size='340' side='right' caption='[[5uhk]], [[Resolution|resolution]] 2.97Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5uhk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UHK FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |
- | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uho|5uho]], [[5uhp|5uhp]], [[5uhl|5uhl]]</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=5uhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uhk OCA], [http://pdbe.org/5uhk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uhk RCSB], [http://www.ebi.ac.uk/pdbsum/5uhk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uhk ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/OGA_HUMAN OGA_HUMAN]] Isoform 1: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:11148210). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714).<ref>PMID:11148210</ref> <ref>PMID:11788610</ref> <ref>PMID:20673219</ref> <ref>PMID:22365600</ref> <ref>PMID:24088714</ref> Isoform 3: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1.<ref>PMID:20673219</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Elsen, N L]] | ||
+ | [[Category: Klein, D J]] | ||
+ | [[Category: Enzyme]] | ||
+ | [[Category: Gh84]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: O-glcnacase]] |
Revision as of 14:05, 29 March 2017
Crystal structure of the core catalytic domain of Human O-GlcNAcase
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Categories: Elsen, N L | Klein, D J | Enzyme | Gh84 | Hydrolase | O-glcnacase