EC Number   |
|---|
    1.1.1.267 | - |
| 1.1.1.267 | apo-form and binary complex with NADPH |
| 1.1.1.267 | docking models for inhibitor (3-[hydroxy(5-oxohexanoyl)amino]propyl)phosphonic acid based on crystal structure in complex with fosmidomycin. Formation of a hydrogen bond between an appropriately placed carbonyl group in the acyl residue and the main-chain NH of M214 located in the flexible catalytic loop of the enzyme |
| 1.1.1.267 | generation of homology model and ligand docking studies |
| 1.1.1.267 | hanging-drop vapour-diffusion method in the presence of NADPH, data to 1.85 A resolution. Space group C2 |
| 1.1.1.267 | homology modeling based on the Escherichia coli homolog |
| 1.1.1.267 | homology modeling of structure |
| 1.1.1.267 | in complex with inhibitor [(1-isoquinolinylamino)methylene]-1,1-bisphosphonate and in complex with inhibitor [[(5-chloro-2-pyridinyl)amino]methylene]-1,1-bisphosphonate |
| 1.1.1.267 | in complex with Mg2+, NADPH, and inhibitor fosmidomycin. Protein exhibits a well-ordered conformation upon substrate binding. No electron density is observed for the nicotinamide-ribose portion of NADPH and the position of D149 anchoring Mg2+ is shifted by NADPH in the active site |
| 1.1.1.267 | in complex with NADPH and Mg2+, and in complex with fosmidomycin, NADPH and Mg2+, both to 2.0 A resolution |
