2x0h: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2x0h]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X0H FirstGlance]. <br> | <table><tr><td colspan='2'>[[2x0h]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X0H FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vvn|2vvn]], [[2wzh|2wzh]], [[2w67|2w67]], [[2wca|2wca]], [[2vvs|2vvs]], [[2j4g|2j4g]], [[2w4x|2w4x]], [[2cho|2cho]], [[2jiw|2jiw]], [[2chn|2chn]], [[2j47|2j47]], [[2wzi|2wzi]], [[2w66|2w66]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vvn|2vvn]], [[2wzh|2wzh]], [[2w67|2w67]], [[2wca|2wca]], [[2vvs|2vvs]], [[2j4g|2j4g]], [[2w4x|2w4x]], [[2cho|2cho]], [[2jiw|2jiw]], [[2chn|2chn]], [[2j47|2j47]], [[2wzi|2wzi]], [[2w66|2w66]]</td></tr> | ||
<tr><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> | <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> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x0h RCSB], [http://www.ebi.ac.uk/pdbsum/2x0h PDBsum]</span></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=2x0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x0h RCSB], [http://www.ebi.ac.uk/pdbsum/2x0h PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/OGA_BACTN OGA_BACTN]] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 35: | Line 37: | ||
[[Category: Bacteroides thetaiotaomicron vpi-5482]] | [[Category: Bacteroides thetaiotaomicron vpi-5482]] | ||
[[Category: Beta-N-acetylhexosaminidase]] | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Davies, G J | [[Category: Davies, G J]] | ||
[[Category: He, Y | [[Category: He, Y]] | ||
[[Category: Glycosidase]] | [[Category: Glycosidase]] | ||
[[Category: Glycoside hydrolase]] | [[Category: Glycoside hydrolase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Inhibitor]] | [[Category: Inhibitor]] | ||
Revision as of 06:09, 25 December 2014
BTGH84 MICHAELIS COMPLEXBTGH84 MICHAELIS COMPLEX
Structural highlights
Function[OGA_BACTN] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedN-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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