EC Number   |
|---|
    2.5.1.72 | both native and SeMet enzyme are crystallized using the hanging-drop vapor-diffusion method at 22°C, structure is determined at 2.8 A resolution |
| 2.5.1.72 | in presence of substrate analogue malate. Diffraction to 2.0 A resolution. Triangular architecture composed of a 3fold repeat of three-layer alphabetaalpha sandwich folding. The active site is located at the interface of the three domains and is centered on the pseudo-3fold axis. The malate molecule is tightly held near the bottom of the active site cavity |
| 2.5.1.72 | mutant K219R/Y107F in complex with the first intermediate resulting from the condensation of dihydroxyacetone phosphate with iminoaspartate and the dihydroxyacetone phosphate analogue phosphoglycolohydroxamate, and mutant K219R/Y21F in complex with quinolinic acid. Phosphoglycolohydroxamate binds to NadA with its phosphate group at the site where the carboxylate groups of the first intermediate also bind |
| 2.5.1.72 | structures of complexes of the Y21F/K219R variant with 4-mercaptophthalic acid, 6-mercaptopyridine-2,3-dicarboxylic acid and 5-mercaptopyrazine-2,3-dicarboxylic acid, at 1.64 A, 1.9 A and 2.1 A resolution, respectively. The carboxylate groups of the inhibitors interact with active site amino acids of His19 and Ser36 (domain 1), Ser124 (domain 2) and His193 and Thr210 (domain 3), and all molecules bind to one iron of the cluster with their thiolate moiety |
| 2.5.1.72 | structures of NadA in complex with dihydroxyacetone phosphate, iminoaspartate analogues, and quinolinate. Dihydroxyacetone phosphate adopts a nearly planar conformation and chelates the [4Fe-4S] cluster via its keto and hydroxyl groups. The cluster may act as a Lewis acid in enediolate formation, like zinc in class II aldolases |
