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Results 1 - 7 of 7
EC Number Crystallization (Commentary)
Show all pathways known for 2.4.2.9Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.9computational docking of inhibitor 5-fluorouracil to the active site of the enzyme. 5-fluorouracil forms hydrogen bonds with residues Tyr192, Gly196, and Leu197 in the complex. 5-fluorouracil shows low average free energy binding with the enzyme which indicates stronger binding than the natural substrate uracil
Show all pathways known for 2.4.2.9Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.9enzyme in complex with UMP, enzyme in complex with CTP, structure with UMP bound in half of the active sites. Hanging-drop vapour-diffusion method
Show all pathways known for 2.4.2.9Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.9hanging drop-vapour diffusion method, enzyme complexed with uracil and 5-phosphoribose 1-diphosphate, 20 mg/ml, mixing of equal volumes, 15 mM sodium citrate/phosphate, 0.2 M NaCl, pH 4.7, 10% polyethylene glycol 3400, X-ray diffraction structure analysis, dynamic light scattering
Show all pathways known for 2.4.2.9Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.9hanging drop-vapour diffusion technique, 2.0 M ammonium phosphate as precipitant, pH 8.0, room temperature, X-ray diffraction structure analysis, crystals are enzymatically active, wild-type and mutant enzymes
Show all pathways known for 2.4.2.9Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.9sitting drop vapor diffusion method, using 0.1 M sodium acetate trihydrate pH 4.6, 1.5 M sodium formate with a 2:1 reservoir-to-protein solution ratio at 25°C
Show all pathways known for 2.4.2.9Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.9two structures of the activated state enzyme in complex with GTP, X-ray diffraction structure determination and analysis at 2.8 A resolution, the first structure which contains PRPP in all active sites, and 2.9 A resolution, for the second structure with PRPP in two sites and the hydrolysis products ribose-5-phosphate and diphosphate in the other sites, respectively, and a third structure of the enzyme in complex with UMP and the allosteric inhibitor CTP
Show all pathways known for 2.4.2.9Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.9vapour diffusion using hanging or sitting drops, room temperature, protein solution 20 mg/ml, pH 7.0, 5 mM phosphate, 0.003 ml + 0.003 ml reservoir solution, pH 7.5, 6-10% polyethylene glycol 4000, 0.1 M HEPES, crystals appeared after 3 weeks, structure determination and analysis
Results 1 - 7 of 7