EC Number |
Reference |
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6.3.2.1 | crystal structure analysis of the enzyme co-crystallized with (2-[(1-benzofuran-2-yl-sulfonyl)carbamoyl]-5-methoxy-1H-indol-1-yl)acetic acid, PDB ID 3IVX, determined at a resolution of 1.73 A, and usage of the structure for enzyme-ligand binding structure predictions in molecular docking |
745786 |
6.3.2.1 | crystal structure of the enzyme complexed with AMP, ATP or beta-alanine |
672114 |
6.3.2.1 | crystal structures of pantothenate synthetase complexed with diphosphomethylphosphonic acid adenosyl ester and pantoate resolved at 1.6 A and of apo Escherichia coli pantothenate synthetase resolved at 1.70 A are used as the initial structures for the simulations |
716880 |
6.3.2.1 | crystal structures with compounds 5-methoxyindole and 2-carboxybenzofuranoic acid bound in a ternary complex and in complex with 2-(2-((benzofuran-2-carboxamido)methyl)-5-methoxy-1H-indol-1-yl)acetic acid |
704206 |
6.3.2.1 | crystals of native PS and PS complexed with alpha,beta-methyleneadenosine 5'-triphosphate, pantoate and the reaction intermediate pantoyl adenylate, crystals are grown by hanging-drop vapor diffusion, 0.003-0.005 ml of PS solution at 10 mg/ml PS is mixed with an equal volume of well solution, best crystals are obtained with well solutions containing 10%-15% polyethylene glycol 3000, 5% glycerol, 2% ethanol, 20 mM MgCl2, 150 mM Li2SO4 and 100 mM imidazole, pH 8.0 at 20°C, crystals diffract to 1.6-2.0 A |
653802 |
6.3.2.1 | native and selenomethionine labeled PS, hanging drop vapor diffusion, hanging drops are composed of equal volumes of PS and reservoir solutions consisting of 50 mM Tris-HCl, pH 8.0, 4%-6% polyethylene glycol 4000, crystals appeare at 19°C after 2-4 days, crystals diffract to 1.7 A |
653927 |
6.3.2.1 | structures of the apoenzyme and the reaction intermediate complex are determined by X-ray crystallography to resolutions of 2.5 A and 1.85 A, respectively. Structural analysis indicate that the apoenzyme adopts an open and relatively mobile structure, while the complex structure is closed and entirely rigid. In the complex structure, pantothenate synthetase and acetate are bound in the active site. Acetate might mimic the substrate beta-alanine. Therefore, the complex structure might represent a catalytic state poised for in-line nucleophilic attack on pantothenate synthetase |
714204 |
6.3.2.1 | tertiary structure of the dimeric N-terminal domain of Escherichia coli pantothenate synthetase, to a resolution of 1.7 A, shows a second molecule of pantoate bound in the ATP-binding pocket. Pantoate binding to the ATP-binding site induces large changes in structure, mainly for backbone and side chain atoms of residues in the ATP binding HXGH(34-37) motif. ATP stoichiometrically displaces pantoate from the ATP-binding site |
703685 |