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2ydq

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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 [http://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 [http://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/"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>
</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>
</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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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cbi|2cbi]], [[2vur|2vur]], [[2x0y|2x0y]], [[2xpk|2xpk]], [[2j62|2j62]], [[2jh2|2jh2]], [[2wb5|2wb5]], [[2v5c|2v5c]], [[2cbj|2cbj]], [[2v5d|2v5d]], [[2yds|2yds]], [[2ydr|2ydr]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://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='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'>[http://proteopedia.org/fgij/fg.htm?mol=2ydq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydq OCA], [http://pdbe.org/2ydq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ydq RCSB], [http://www.ebi.ac.uk/pdbsum/2ydq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ydq 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=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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[[http://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1]] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. [[http://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. [[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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 2ydq" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2ydq" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[O-GlcNAcase|O-GlcNAcase]]
== References ==
== References ==
<references/>
<references/>

Revision as of 12:27, 27 April 2022

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

PDB ID 2ydq

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