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Results 1 - 10 of 10
EC Number Crystallization (Commentary) Reference
Show all pathways known for 2.6.1.62Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.62- 637095
Show all pathways known for 2.6.1.62Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.62complex of holoenzyme and 7-keto-8-aminopelargonic acid 637097
Show all pathways known for 2.6.1.62Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.62crystallization of the native and the selenomethionine enzyme, without ligand in two different space groups. In both cases, the structures show a dimer made of two monomers related by a noncrystallographic twofold axis 723412
Show all pathways known for 2.6.1.62Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.62hanging drop vapor diffusion method 637096
Show all pathways known for 2.6.1.62Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.62in complex with inhibitors 5-(pyridin-2-yl)thiophene-2-carboxamide, 4-(1H-imidazol-1-yl)benzamide, and N-methyl-1-[4-(1H-pyrazol-1-ylmethyl)phenyl]methanamine 738841
Show all pathways known for 2.6.1.62Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.62in complex with substrate 7-oxo-8-aminopelargonic acid and in complex with inhibitors 1-(1,3-benzothiazol-2-yl)methanamine and 2-hydrazinyl-1,3-benzothiazole. The side chains of Tyr25, Trp65, Arg400, and Tyr407 are shown to be quite flexible. Small molecule binding induces unexpected conformational remodeling in the substrate binding site 738054
Show all pathways known for 2.6.1.62Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.62native and the selenomethionine enzyme without ligand, in two different space groups. The structures show a dimer made of two monomers related by a noncrystallographic twofold axis 723412
Show all pathways known for 2.6.1.62Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.62purified recombinant enzyme, sitting drop vapor diffusion method, mixing of 11 mg/ml protein in 50 mM Tris, 100 mM NaCl, and 0.02 mM PLP, pH 7.9, with precipitant solution containing 0.1 M sodium citrate, pH 6.1, 0.2 M potassium sodium tartrate, and 1.8 M ammonium sulfate. A glass capillary containing 0.008 ml of protein solution is mounted in the gel tube with 1% agarose presoaked in 1 ml of the precipitant solution, method optimization, 1 month at 20°C. X-ray diffraction structure determination and analysis at 1.6 A resolution 758685
Show all pathways known for 2.6.1.62Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.62purified recombinant mutant enzymes Y17F, Y144F, D147N, R253A, and R253K, hanging drop method, 20°C, 10 mg/ml protein in solution mixed with equal volume of well solution containing 26-28% PEG 4000, 9-12% methylpentanediol, 100 mM HEPES, pH 7.5, microseeding, 2 days, X-ray diffraction structure determination and analysis at 1.7-2.4 A resolution, modeling 661088
Show all pathways known for 2.6.1.62Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.62to 2.2 A resolution, by molecular replacement, and superimposition of the structures bound either to the S-adenosyl-L-methionine analog sinefungin or to 7-oxo-8-aminopelargonic acid. Comparison to structure of the Bacillus subtilis enzyme, EC 2.5.1.105 714208
Results 1 - 10 of 10