EC Number   |
|---|
    3.5.2.3 | - |
| 3.5.2.3 | at 2.2 A |
| 3.5.2.3 | complex of aspartate transcarbamoylase and dihydroorotase |
| 3.5.2.3 | crystal structure analysis of the zinc environment at ambient pressure, at 600 bar, and at 1200 bar |
| 3.5.2.3 | crystallized without ligand and in the presence of the inhibitors 2-oxo-1,2,3,6-tetrahydropyrimidine-4,6-dicarboxylate and 5-fluoroorotate, hanging drop vapour diffusion method with 15-20% (w/v) polyethylene glycol 3350, 0.1 M MES (pH 6.0-6.5), 75 mM MgCl2, 150 mM KCl (with ligand) or 20-25% polyethylene glycol 3350, 0.1 M Na HEPES (pH 7) and 0.2 M NaF (without ligand) |
| 3.5.2.3 | hanging drop method, monoclinic structure has a novel cysteine ligand to the zinc that blocks the active site and functions as a cysteine switch, active site residues are located in disordered loops, which may function as a disorder-to-order entropy switch |
| 3.5.2.3 | hanging drop vapour diffusion method with 15-20% polyethylene glycol 3350, 0.1 M MES, pH 6.0-6.5, 75 mM MgCl2, and 150 mM KCl |
| 3.5.2.3 | human DHOase domain K1556A mutant, hanging drop vapor diffusion method, mixing of 20 mg/ml protein in 20 mM HEPES and 100 mM NaCl, pH 7.0, with reservoir solution containing 2 M sodium chloride, 100 mM MES, 200 mM sodium acetate, pH 6.5, at room temperature, X-ray diffraction structure determination and analysis at 2.77 A resolution |
| 3.5.2.3 | in complex with 5-fluoroorotate, hanging drop vapour diffusion method 14-16% PEG 3350, 0.1 M MES pH 6.25, 25 mM MgCl2, 0.2 M KCl and 30% sucrose |
| 3.5.2.3 | in the presence of enantiomerically pure L-dihydroorotate, refined at 1.9 Angstrom resolution |
