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EC Number Crystallization (Commentary)
Show all pathways known for 4.6.1.12Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.12-
Show all pathways known for 4.6.1.12Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.123.1 A resolution crystal structure of the Met142/Leu144 mutant
Show all pathways known for 4.6.1.12Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.12computational model of binding of inhibitor N-[4-[(6-aminopyridin-3-yl)amino]-3-methylbenzyl]-4-(trifluoromethyl)benzamide in the active site
Show all pathways known for 4.6.1.12Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.12crystals grow in space group P4(1)2(1)2 from polyethylene glycol using the hanging-drop method
Show all pathways known for 4.6.1.12Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.12hanging drop vapor diffusion method
Show all pathways known for 4.6.1.12Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.12hanging drop vapor diffusion method, crystal structure of IspDF, a bifunctional methylerythritol 4-phosphate cytidyltransferase methylerythritol 2,4-cyclodidiphosphate synthase
Show all pathways known for 4.6.1.12Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.12hanging-drop vapour diffusion method, X-ray crystal structures refined to 2.8 A resolution. The first structure contains a bound Mn2+ cation and the second structure contains CMP, 2-C-methyl-D-erythritol-2,4-cyclodiphosphate, and Mn2+
Show all pathways known for 4.6.1.12Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.12high-resolution structure, 16 A, of the enzyme in absence of substrate in the active site. Optimized crystals are obtained at a protein concentration of 35 mg/ml in a solution containing 4 M sodium formate and 5% glycerol. The crystals grow to avarage dimensions of 0.4 * 0.3 * 0.3 mM within a week
Show all pathways known for 4.6.1.12Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.12in complex with cytidine 5-monophosphate, at 2.3 A resolution. In contrast to bacterial enzymes, the cavity of Arabidopsis thaliana structure is unsuited for binding a diphosphate moiety
Show all pathways known for 4.6.1.12Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.12IspF-CDP complex, to 1.8 A resolution. IspF in complex with compound 6b, to 3.1 A resolution, belongs to space group I213 with unit cell parameter a = 144 A. IspF in complex with compound 7, to 2.7 A resolution, belongs to space group I213 with unit cell parameter a = 144.5 A. IspF in complex with cytosine arabinoside monophosphate, to 2.1 A resolution, belongs to space group P21 with unit cell parameters a = 88.8 A, b = 54.2 A, c = 118.4 A, beta = 95°. IspF in complex with 5-fluorocytidine, to 2.5 A resolution, belongs to space group C2 with unit cell parameters a = 104.68 A, b = 54.83 A, c = 88.51 A, beta = 99.66°. IspF in complex with cidofovir, to 2.8 A resolution, belongs to space group I213 with unit cell parameter a = 145.68 A
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