1QH6
CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE
Summary for 1QH6
Entry DOI | 10.2210/pdb1qh6/pdb |
Related | 1QH7 |
Descriptor | XYLANASE, beta-D-xylopyranose-(1-4)-2-deoxy-2-fluoro-alpha-D-xylopyranose (3 entities in total) |
Functional Keywords | glycosyl hydrolase, hydrolase |
Biological source | Bacillus agaradhaerens |
Total number of polymer chains | 2 |
Total formula weight | 46879.57 |
Authors | Sabini, E.,Sulzenbacher, G.,Dauter, M.,Dauter, Z.,Jorgensen, P.L.,Schulein, M.,Dupont, C.,Davies, G.J.,Wilson, K.S. (deposition date: 1999-05-11, release date: 2000-05-17, Last modification date: 2023-12-27) |
Primary citation | Sabini, E.,Sulzenbacher, G.,Dauter, M.,Dauter, Z.,Jorgensen, P.L.,Schulein, M.,Dupont, C.,Davies, G.J.,Wilson, K.S. Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase. Chem.Biol., 6:483-492, 1999 Cited by PubMed: 10381409DOI: 10.1016/S1074-5521(99)80066-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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