5uhp

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'''Unreleased structure'''
 
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The entry 5uhp is ON HOLD until Paper Publication
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==Crystal structure of the core catalytic domain of human O-GlcNAcase==
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<StructureSection load='5uhp' size='340' side='right' caption='[[5uhp]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5uhp]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UHP FirstGlance]. <br>
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Description:
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</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>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uho|5uho]], [[5uhl|5uhl]], [[5uhk|5uhk]]</td></tr>
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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=5uhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uhp OCA], [http://pdbe.org/5uhp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uhp RCSB], [http://www.ebi.ac.uk/pdbsum/5uhp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uhp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Elsen, N L]]
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[[Category: Klein, D J]]
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[[Category: Enzyme]]
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[[Category: Gh84]]
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[[Category: Hydrolase]]
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[[Category: O-glcnacase]]

Revision as of 14:05, 29 March 2017

Crystal structure of the core catalytic domain of human O-GlcNAcase

5uhp, resolution 2.79Å

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