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EC Number Crystallization (Commentary) Reference
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7at 19°C, from 10 mM MES, pH 6.4, 10% (w/v) polyethylene glycol 20000, in the presence of 5 mM UDP-N-acetyl-D-glucosamine and 5 mM phosphoenolpyruvate 674498
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7crystallization of substrate-free enzyme, two-domain structure with an unusual fold, inside out alpha/beta barrel, which is built up from the 6fold repetititon of one folding unit, structure analysis 637600
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7crystallization of the enzyme complexed with UDP-N-acetylglucosamine and fosfomycin, two-domain structure with the active site located between them, structure and substrate binding analysis 637599
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7in complex with inhibitor cnicin and substrate UDP-N-acetylglucosamine, at 2.0 A resolution. The enzyme catalyzes the formation of a covalent adduct between cnicin and UDP-N-acetylglucosamine via an anti-Michael 1,3-addition of UDP-N-acetylglucosamine to an alpha,beta-unsaturated carbonyl function in cnicin thus forming a noncovalent suicide inhibitor 688290
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7in complex with inhibitor T6361 659457
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7in complex with substrates, hanging drop vapor diffusion method, using 0.1 M Bis-Tris (pH 5.5), 0.2 M NH4OAc, 25% (w/v) PEG 3350 722746
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7in complex with UDP-N-acetylglucosamine and fosfomycin, sitting drop vapor diffusion method, using 25% (w/v) PEG 3350, 0.1 M bis-Tris pH 6.5 721232
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7in complex with UDP-N-acetylglucosamine and fosfomycin, to 2.3 A resolution. The active-site loop can adopt one of the three major conformations: a fully open conformation, a half-open conformation, and a closed conformation. Fosfomycin can bind without inducing a large change in the half-open conformation of the binary complex with UDP-N-acetylglucosamine 689975
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7in the apo-form, as well as in a complex with UDP-N-acetylglucosamine and fosfomycin using ammonium sulfate as the precipitant, hanging drop vapour diffusion method 675932
Show all pathways known for 2.5.1.7Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.7MurA is crystallized in the presence of sodium phosphite and UDP-N-acetylmuramic acid using the hanging drop vapor diffusion method, the MurA cocrystal structure with UDP-N-acetylmuramic acid and phosphite reveals a new staged MurA conformation in which the Arg397 side chain tracked phosphite out of the catalytic site 702267
Results 1 - 10 of 12 > >>