EC Number |
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2.4.2.9 | computational 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 |
2.4.2.9 | enzyme in complex with UMP, enzyme in complex with CTP, structure with UMP bound in half of the active sites. Hanging-drop vapour-diffusion method |
2.4.2.9 | hanging 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 |
2.4.2.9 | hanging 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 |
2.4.2.9 | sitting 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 |
2.4.2.9 | two 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 |
2.4.2.9 | vapour 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 |