EC Number   |
Reference |
|---|
    1.5.1.2 | 2.8 A resolution structure of the pyrroline-5-carboxylate reductase apo enzyme, and its ternary complex with NADPH and substrate analog at 3.1 A |
675382 |
| 1.5.1.2 | binary complexes of PYCR1 with NADPH or proline, at 1.9 A resolution, and a ternary complex containing NADPH and a P5C/proline analog, to 1.85 A resolution. NADPH is bound to the Rossmann fold. Structures provide a model of the Michaelis complex formed during hydride transfer |
740763 |
| 1.5.1.2 | crystal structure is determined at 2.0 A resolution, in complex with NADP+ at 2.1 A resolution |
675361 |
| 1.5.1.2 | crystal structure is determined at 2.15 A resolution in complex with NADP+, and at 2.20 A in complex with L-proline |
675361 |
| 1.5.1.2 | crystal structures of unliganded P5CR decamer, and its complexes with the products NAD+, NADP+, and L-proline, to 1.7, 1.85, 1.95, and 2.1 A resolution, respectively |
740491 |
| 1.5.1.2 | diffraction to 3.5 A resolution |
701063 |
| 1.5.1.2 | PYCR1 complexed with N-formyl-L-proline, inhibitor binding is accompanied by conformational changes in the active site, including the translation of an alpha-helix by 1 A |
763270 |
| 1.5.1.2 | the protein is crystallized by the hanging-drop vapor-diffusion method at 37°C and diffraction data are obtained to a resolution of 2.8 A |
676969 |
