EC Number   |
|---|
    3.1.3.3 | apo-form and in complex with its substrate L-phosphoserine, to 1.5 A and 1.8 A resolution, respectively. In the crystal structure of the enzyme-substrate complex, oxygen atoms of the carboxyl group of L-phosphoserine form hydrogen bonds with main-chain amides of Gln21 and Gly22, and Nepsilon2 of Gln21, and partly form a hydrogen or an ionic bond withNepsilon2 of His85. The nitrogen atom of amino group of L-phosphoserine forms a hydrogen or an ionic bond with oxygen atoms of the side-chain carboxyl group of Glu82, and forms hydrogen bonds with Nepsilon2 of His85 and Ogamma1 of Thr15 |
| 3.1.3.3 | construction of a homology model and molecular docking of O-phospho-L-serine. Residues Asp185, Ser273, Lys-318, and Asp-341 are part of the substrate binding pocket. Val186 and Ser188 might also interact with O-phospho-L-serine |
| 3.1.3.3 | crystals are grown by using the hanging drop vapor diffusion method with seeding.1.5 A resolution the X-ray crystal structure of the complex of BeF3 2 with phosphoserine phosphatase. The structure is comparable to that of a phosphoenzyme intermediate: BeF3- is bound to Asp11 with the tetrahedral geometry of a phosphoryl group, is coordinated to Mg2+, and is bound to residues surrounding the active site that are conserved in the haloacid dehalogenase (HAD) superfamily |
| 3.1.3.3 | hanging drop vapour-diffusion method. A resolution of 1.53 A provides a detailed model of the active site in a completely open conformation and the water molecules bound to it |
| 3.1.3.3 | hanging-drop vapor-diffusion method, crystal structure determined at 1.8 A resolution |
| 3.1.3.3 | hanging-drop vapour diffsuion method |
| 3.1.3.3 | hanging-drop vapour diffusion method |
| 3.1.3.3 | hanging-drop vapour-diffusion method |
| 3.1.3.3 | high-resolution, 1.5-1.9 A structures which define the open state prior to substrate binding, the complex with phosphoserine substrate bound, and the complex with AlF3, a transition-state analog for the phospho-transfer steps in the reaction |
| 3.1.3.3 | replacement of sixfold coordinated Mg2+ in active site by Ca2+ results in sevenfold coordinated metal ion, explaining the inhibitory effect of Ca2+ |
