EC Number   |
|---|
    1.5.99.B2 | - |
| 1.5.99.B2 | analysis of the three-dimensional model of TtProDH crystal structure, PDB ID 2G37 |
| 1.5.99.B2 | beta subunit is the L-proline dehydrogenase catalytic component and contains FAD, alpha subunit has a classical dinucleotide fold domain with ATP and a Cys-clustered domain. FMN is located at the interface of alpha and beta subunits |
| 1.5.99.B2 | crystal structure of PDH1, which is a heterooctameric complex containing three different cofactors: FAD, FMN, and ATP. The structure is determined by x-ray crystallography to a resolution of 2.86 A. The structure of the beta subunit, which is an L-proline dehydrogenase catalytic component containing FAD as a cofactor, is similar to that of monomeric sarcosine oxidase |
| 1.5.99.B2 | enzyme bound with L-proline, sitting drop vapor diffusion method, using 0.2 M ammonium acetate, 0.1 M trisodium citrate dihydrate (pH 5.6), and 30% (w/v) polyethylene glycol 4000 |
| 1.5.99.B2 | enzyme in the oxidized state complexed with the proline analogue L-tetrahydrofuroic acid and in the reduced state with the proline site vacant, sitting drop vapor diffusion method, using 0.2 M MgCl2, 25% (w/v) PEG 3350, and 0.1 mM Bis-Tris (pH 5.8), at 22°C |
| 1.5.99.B2 | from a monodisperse protein solution with detergent n-octyl beta-D-glucopyranoside |
| 1.5.99.B2 | His-tag removed, three crystal forms: apparent tetragonal, hexagonal and centered monoclinic |
| 1.5.99.B2 | sitting drop vapour diffusion method, with 100 mM imidazole (pH 7), 100 mM MgCl2, 17% 2-methyl-2,4-pentanediol, and 5 mM dithiothreitol |
| 1.5.99.B2 | sitting drop vapour diffusion method, with 100 mM imidazole buffer at pH 7, 100 mM MgCl2, 14% 2-methyl-2,4-pentanediol, and 5 mM dithiothreitol |
