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5uhl

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==Crystal structure of the core catalytic domain of human O-GlcNAcase complexed with Thiamet G==
==Crystal structure of the core catalytic domain of human O-GlcNAcase complexed with Thiamet G==
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<StructureSection load='5uhl' size='340' side='right' caption='[[5uhl]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
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<StructureSection load='5uhl' size='340' side='right'caption='[[5uhl]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[5uhl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5UHL FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.14&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uho|5uho]], [[5uhp|5uhp]], [[5uhk|5uhk]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
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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=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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5uhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uhl OCA], [https://pdbe.org/5uhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uhl RCSB], [https://www.ebi.ac.uk/pdbsum/5uhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uhl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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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[https://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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==See Also==
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*[[O-GlcNAcase|O-GlcNAcase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Elsen, N L]]
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[[Category: Homo sapiens]]
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[[Category: Klein, D J]]
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[[Category: Large Structures]]
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[[Category: Enzyme]]
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[[Category: Elsen NL]]
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[[Category: Gh84]]
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[[Category: Klein DJ]]
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[[Category: Hydrolase]]
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[[Category: O-glcnacase]]
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[[Category: Thiamet g]]
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Current revision

Crystal structure of the core catalytic domain of human O-GlcNAcase complexed with Thiamet G

PDB ID 5uhl

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