EC Number   |
Reference |
|---|
    1.2.1.88 | - |
392041, 740867 |
| 1.2.1.88 | apoenzyme and in complex with NAD+, to 1.95 and 2.17 A resolution, respectively |
740061 |
| 1.2.1.88 | complexed with glutarate, succinate, malonate, glyoxylate, and acetate |
739954 |
| 1.2.1.88 | mutants R100A crystallizes in the same lattice as wild-type, mutant R100A/K104A/R111A crystaLLIZES IN space group P1 |
740867 |
| 1.2.1.88 | purified ZmALDH12 in complex with NAD+, sitting drop vapour diffusion method, mixing of 2 mg/ml protein in 50 mM Tris, pH 7.8, 50 mM NaCl, 0.5 mM tris(2-caboxyethyl)phosphine (TCEP), 1 mM NAD+, and 5% v/v glycerol with a crystallization solution containing 0.09 M sodium nitrate, sodium phosphate, and ammonium sulfate, and a precipitant mixture containing 25% v/v 2-methyl-2,4-pentanediol, 25% w/v PEG 1000, and 25% w/v polyethylene glycol 3350, and 0.1 M Tris/bicine pH 8.5, in a 1:1 ratio v/v, X-ray diffraction structure determination and analysis at 2.20 A resolution, structure modeling using molecular replacement and a search model derived from a betaine ALDH (PDB ID 4MPY) |
763363 |
| 1.2.1.88 | PutA with the following ligands bound in the GSALDH active site: NADH, D-proline, trans-4-hydroxy-D-proline, cis-4-hydroxy-D-proline, L-proline, and trans-4-hydroxy-L-proline, sitting drop vapor diffusion method, using 19% (w/v) PEG-3350, 0.2 M ammonium sulfate, 0.1 M magnesium chloride, 0.1 M HEPES (pH 8.0), and 0.1 M sodium formate |
762677 |
| 1.2.1.88 | space group P21 with eight molecules in the asymmetric unit |
740867 |
| 1.2.1.88 | the substrate-free form displays multiple active site conformations. Protein forms a trimer-of-dimers hexamer in solution |
740061 |
| 1.2.1.88 | unligandend form and in complex with NAD+, NADPH, and with product glutamate |
675402 |
