1UZB
1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| A | 0004657 | molecular_function | proline dehydrogenase activity |
| A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| A | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| B | 0004657 | molecular_function | proline dehydrogenase activity |
| B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| B | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MRD A1517 |
| Chain | Residue |
| A | ARG147 |
| A | ALA148 |
| A | LEU500 |
| A | HOH2033 |
| A | HOH2343 |
| A | HOH2354 |
| A | HOH2749 |
| B | GLU158 |
| B | VAL160 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD A1518 |
| Chain | Residue |
| A | LEU275 |
| A | GLN279 |
| A | HOH2750 |
| A | HOH2751 |
| A | HOH2752 |
| B | MRD1518 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MRD B1517 |
| Chain | Residue |
| A | GLU158 |
| A | HOH2373 |
| B | PHE6 |
| B | TYR144 |
| B | ARG147 |
| B | ALA148 |
| B | HOH2316 |
| B | HOH2716 |
| B | HOH2718 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD B1518 |
| Chain | Residue |
| A | MRD1518 |
| B | GLU416 |
| B | HOH2719 |
| B | HOH2720 |
| B | HOH2721 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MRD B1519 |
| Chain | Residue |
| B | GLN279 |
| B | HOH2722 |
| B | HOH2723 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MRD B1520 |
| Chain | Residue |
| A | PHE170 |
| A | VAL172 |
| A | LYS510 |
| A | HOH2113 |
| A | HOH2241 |
| A | HOH2242 |
| B | ARG461 |
| B | ARG462 |
| B | PHE464 |
| B | HIS465 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YgFQGQKCSAAS |
| Chain | Residue | Details |
| A | TYR315-SER326 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. VETGGKNA |
| Chain | Residue | Details |
| A | VAL287-ALA294 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | CYS322 | |
| A | ASN184 | |
| A | GLU288 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| B | CYS322 | |
| B | ASN184 | |
| B | GLU288 |
