5uhl: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5uhl is ~~ON HOLD~~ ~~until Paper Publication~~

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

~~Authors~~:

== 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 guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UHL FirstGlance].

~~Description~~:

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</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: ~~Unreleased Structures~~]]

<tr id='related'><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[5uho|5uho]], [[5uhp|5uhp]], [[5uhk|5uhk]]</td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[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]</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 ==

__TOC__

</StructureSection>

[[Category: Elsen, N L]]

[[Category: Klein, D J]]

[[Category: Enzyme]]

[[Category: Gh84]]

[[Category: Hydrolase]]

[[Category: O-glcnacase]]

[[Category: Thiamet g]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5uhl is ON HOLD  until Paper Publication
+==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]] 3.14&Aring;' scene=''>
-Authors:
+== 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>
-Description:
+</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: Unreleased Structures]]
+<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]]