2ydq

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Current revision (14:03, 1 February 2024) (edit) (undo)
 
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<StructureSection load='2ydq' size='340' side='right'caption='[[2ydq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='2ydq' size='340' side='right'caption='[[2ydq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ydq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YDQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ydq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YDQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cbi|2cbi]], [[2vur|2vur]], [[2x0y|2x0y]], [[2xpk|2xpk]], [[2j62|2j62]], [[2jh2|2jh2]], [[2wb5|2wb5]], [[2v5c|2v5c]], [[2cbj|2cbj]], [[2v5d|2v5d]], [[2yds|2yds]], [[2ydr|2ydr]]</div></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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=2ydq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydq OCA], [https://pdbe.org/2ydq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ydq RCSB], [https://www.ebi.ac.uk/pdbsum/2ydq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ydq ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ydq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydq OCA], [https://pdbe.org/2ydq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ydq RCSB], [https://www.ebi.ac.uk/pdbsum/2ydq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ydq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1]] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. [[https://www.uniprot.org/uniprot/NCOAT_HUMAN NCOAT_HUMAN]] Cleaves GlcNAc but not GalNAc from glycopeptides. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc. Possesses hyaluronidase activity. Acetylates 'Lys-8' of histone H4 and 'Lys-14' of histone H3.<ref>PMID:11148210</ref> <ref>PMID:11788610</ref>
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[https://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus perfringens veillon and zuber 1898]]
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[[Category: Clostridium perfringens]]
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[[Category: Beta-N-acetylhexosaminidase]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Aalten, D M.F van]]
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[[Category: Borodkin VS]]
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[[Category: Borodkin, V S]]
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[[Category: Gray LJ]]
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[[Category: Gray, L J]]
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[[Category: Schimpl M]]
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[[Category: Schimpl, M]]
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[[Category: Van Aalten DMF]]
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[[Category: Hydrolase-peptide complex]]
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Current revision

CpOGA D298N in complex with hOGA-derived O-GlcNAc peptide

PDB ID 2ydq

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