2X0H
BtGH84 Michaelis complex
Summary for 2X0H
Entry DOI | 10.2210/pdb2x0h/pdb |
Related | 2CHN 2CHO 2J47 2J4G 2JIW 2VVN 2VVS 2W4X 2W66 2W67 2WCA 2WZH 2WZI |
Descriptor | O-GLCNACASE BT_4395, 3,4-difluorophenyl 2-deoxy-2-[(difluoroacetyl)amino]-beta-D-glucopyranoside, GLYCEROL, ... (5 entities in total) |
Functional Keywords | glycoside hydrolase, hydrolase, inhibitor, glycosidase |
Biological source | BACTEROIDES THETAIOTAOMICRON VPI-5482 |
Total number of polymer chains | 2 |
Total formula weight | 170507.02 |
Authors | He, Y.,Davies, G.J. (deposition date: 2009-12-08, release date: 2010-01-26, Last modification date: 2023-12-20) |
Primary citation | He, Y.,Macauley, M.S.,Stubbs, K.A.,Vocadlo, D.J.,Davies, G.J. Visualizing the Reaction Coordinate of an O-Glcnac Hydrolase J.Am.Chem.Soc., 132:1807-, 2010 Cited by PubMed Abstract: 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. PubMed: 20067256DOI: 10.1021/JA9086769 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.21 Å) |
Structure validation
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