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Results 1 - 7 of 7
EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.113-
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.113crystals of both the native protein and the protein-inhibitor complex. Superimpositions are performed with LSQMAN. Comparison with human alpha-1,2-mannosidase–thiodisaccharide complex
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.113hanging drop vapor diffusion method, 15 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.113in complex with kifunensine
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.113in complex with the substrate analogue methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside, to 1.95 A resolution. The intact disaccharide spans the ?1/+1 subsites, with the D-lyxoside ring in the -1 subsite in the 1C4 chair conformation.The absence of the C5' hydroxymethyl group on the D-lyxoside moiety results in the side chain of Arg407 adopting two alternative conformations, the minor one interacting with Asp375 and the major one interacting with both the D-lyxoside and the catalytic base Glu409, thus disrupting its function
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.113modeling of structure at 2.2 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.113native enzyme and in complexes with the inhibitors 1-deoxymannojirimycin and kifunensine, hanging drop vapor diffusion method, using 17-22% (w/v) polyethylene glycol 6000, 50 mM KH2PO4, pH 4.6
Results 1 - 7 of 7