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2x0h

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'''Unreleased structure'''
 
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The entry 2x0h is ON HOLD until Paper Publication
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==BtGH84 Michaelis complex==
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<StructureSection load='2x0h' size='340' side='right'caption='[[2x0h]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2x0h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X0H FirstGlance]. <br>
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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]] 2.21&#8491;</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=14T:3,4-DIFLUOROPHENYL+2-DEOXY-2-[(DIFLUOROACETYL)AMINO]-BETA-D-GLUCOPYRANOSIDE'>14T</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2x0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0h OCA], [https://pdbe.org/2x0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x0h RCSB], [https://www.ebi.ac.uk/pdbsum/2x0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x0h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/OGA_BACTN OGA_BACTN] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x0/2x0h_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2x0h ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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N-Acetylglucosamine beta-O-linked to serine and threonine residues of nucleocytoplasmic proteins (O-GlcNAc) has been linked to neurodegeneration, cellular stress response, and transcriptional regulation. Removal of O-GlcNAc is catalyzed by O-GlcNAcase (OGA) using a substrate-assisted catalytic mechanism. Here we define the reaction coordinate using chemical approaches and directly observe both a Michaelis complex and the oxazoline intermediate.
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Authors: He, Y., Davies, G.J.
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Visualizing the Reaction Coordinate of an O-GlcNAc Hydrolase.,He Y, Macauley MS, Stubbs KA, Vocadlo DJ, Davies GJ J Am Chem Soc. 2010 Jan 12. PMID:20067256<ref>PMID:20067256</ref>
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Description: BtGH84 Michaelis complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2x0h" style="background-color:#fffaf0;"></div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 23 09:12:52 2009''
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==See Also==
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*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
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*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
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*[[O-GlcNAcase|O-GlcNAcase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacteroides thetaiotaomicron VPI-5482]]
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[[Category: Large Structures]]
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[[Category: Davies GJ]]
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[[Category: He Y]]

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BtGH84 Michaelis complex

PDB ID 2x0h

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