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5uhl
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the core catalytic domain of human O-GlcNAcase complexed with Thiamet G== | |
| - | + | <StructureSection load='5uhl' size='340' side='right' caption='[[5uhl]], [[Resolution|resolution]] 3.14Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5uhl]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UHL FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8BJ:(2Z,3AR,5R,6S,7R,7AR)-2-(ETHYLIMINO)-5-(HYDROXYMETHYL)HEXAHYDRO-3AH-PYRANO[3,2-D][1,3]THIAZOLE-6,7-DIOL'>8BJ</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uho|5uho]], [[5uhp|5uhp]], [[5uhk|5uhk]]</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=5uhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uhl OCA], [http://pdbe.org/5uhl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uhl RCSB], [http://www.ebi.ac.uk/pdbsum/5uhl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uhl 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]] | ||
| + | [[Category: Thiamet g]] | ||
Revision as of 14:05, 29 March 2017
Crystal structure of the core catalytic domain of human O-GlcNAcase complexed with Thiamet G
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Categories: Elsen, N L | Klein, D J | Enzyme | Gh84 | Hydrolase | O-glcnacase | Thiamet g
