2BJA
Crystal Analysis of 1-Pyrroline-5-Carboxylate Dehydrogenase from Thermus with bound NADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 2 |
| Details | BINDING SITE FOR RESIDUE CL A1519 |
| Chain | Residue |
| A | HIS465 |
| B | LYS510 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B1519 |
| Chain | Residue |
| A | LYS510 |
| B | HIS465 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD A1517 |
| Chain | Residue |
| A | GLU210 |
| A | GLY240 |
| A | GLU241 |
| A | ALA245 |
| A | PHE258 |
| A | SER261 |
| A | VAL264 |
| A | ACT1518 |
| A | HOH2411 |
| A | HOH2412 |
| A | HOH2413 |
| A | HOH2414 |
| A | ILE180 |
| A | ALA181 |
| A | TRP183 |
| A | LYS207 |
| A | ALA209 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A1518 |
| Chain | Residue |
| A | ALA245 |
| A | GLU249 |
| A | LYS267 |
| A | ALA271 |
| A | NAD1517 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MRD A1520 |
| Chain | Residue |
| A | PHE6 |
| A | TYR144 |
| A | ARG147 |
| A | ALA148 |
| A | HOH2009 |
| A | HOH2161 |
| A | HOH2415 |
| A | HOH2416 |
| B | GLU158 |
| B | VAL160 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAD B1517 |
| Chain | Residue |
| B | ILE180 |
| B | ALA181 |
| B | TRP183 |
| B | LYS207 |
| B | ALA209 |
| B | GLU210 |
| B | GLY240 |
| B | GLY244 |
| B | ALA245 |
| B | PHE258 |
| B | SER261 |
| B | VAL264 |
| B | ACT1518 |
| B | HOH2388 |
| B | HOH2389 |
| B | HOH2390 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B1518 |
| Chain | Residue |
| B | ALA245 |
| B | GLU249 |
| B | ILE268 |
| B | ALA271 |
| B | NAD1517 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD B1520 |
| Chain | Residue |
| A | GLU158 |
| A | HOH2181 |
| B | PHE6 |
| B | TYR144 |
| B | ARG147 |
| B | ALA148 |
| B | HOH2146 |
| B | HOH2391 |
| B | HOH2392 |
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. VETGGKDA |
| Chain | Residue | Details |
| A | VAL287-ALA294 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | ASN184 | |
| A | GLU288 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| B | ASN184 | |
| B | GLU288 |
