EC Number   |
|---|
    3.2.1.21 | 1.69 A resolution |
| 3.2.1.21 | 2.4 and 2.3 A resolution, complexed with gluconate ligand |
| 3.2.1.21 | 2.7 A resolution |
| 3.2.1.21 | 3.3 A resolution |
| 3.2.1.21 | at a resolution of 2.05A. It is composed of an (alpha/beta)8 domain similar to a triose phosphate isomerase barrel, a five-stranded alpha/beta sandwich domain (both of which are important for active-site organization), and a C-terminal fibronectin type III |
| 3.2.1.21 | covalent intermediate of mutant E165P, in which glucose is bound to nucleophile E373. Structure confirms a double displacement mechanism |
| 3.2.1.21 | crystal structure of mutant E191D,F198V is determined at 1.9 A resolution in complex with DIMBOA-glucoside |
| 3.2.1.21 | free enzyme and its covalent intermediate with 2-deoxy-2-fluoroglucoside at 2.2 A and 1.55 A resolution, respectively. The complex with the 2-fluoroglucoside includes a glycerol molecule, which may make a nucleophilic attack on the anomeric carbon in a transglycosylation reaction. Sugars are positioned as acceptors for transglycosylation by their interactions with E176, the catalytic acid/base, and Y131. Residues I179, N190 and N245 appear to interact with the substrates |
| 3.2.1.21 | hanging drop vapor diffusion method, using 0.04 M potassium dihydrogen phosphate pH 5.1, 16% (w/v) PEG 8000, and 20% (v/v) glycerol, at 20°C |
| 3.2.1.21 | in complex with a covalent intermediate, 2-deoxy-2-fluoroglucoside and, n-octyl-beta-D-thioglucopyranoside, microbatch under oil method, using 0.1 M Bis-Tris, pH 6.5, and 20% PEG MME 5000 |
