2J5N
1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS THERMOPHIRUS WITH BOUND INHIBITOR GLYCINE AND NAD.
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 | 8 |
| Details | BINDING SITE FOR RESIDUE GLY A 1517 |
| Chain | Residue |
| A | SER323 |
| A | GLY477 |
| A | ALA478 |
| A | PHE485 |
| A | HOH2246 |
| A | HOH2529 |
| A | HOH2541 |
| A | HOH2572 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD A 1518 |
| Chain | Residue |
| A | ALA181 |
| A | PRO182 |
| A | TRP183 |
| A | ASN184 |
| A | ILE189 |
| A | LYS207 |
| A | ALA209 |
| A | GLU210 |
| A | GLY240 |
| A | GLU241 |
| A | GLY244 |
| A | ALA245 |
| A | PHE258 |
| A | THR259 |
| A | GLY260 |
| A | SER261 |
| A | VAL264 |
| A | GLU288 |
| A | THR289 |
| A | GLY290 |
| A | CYS322 |
| A | GLU417 |
| A | PHE419 |
| A | PHE485 |
| A | ACT1519 |
| A | HOH2323 |
| A | HOH2324 |
| A | HOH2573 |
| A | HOH2574 |
| A | HOH2575 |
| A | HOH2576 |
| A | HOH2577 |
| A | HOH2578 |
| A | HOH2579 |
| A | ILE180 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 1519 |
| Chain | Residue |
| A | ALA245 |
| A | GLU249 |
| A | ALA271 |
| A | NAD1518 |
| A | HOH2580 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 1520 |
| Chain | Residue |
| A | ARG462 |
| A | PHE464 |
| A | HIS465 |
| A | HOH2581 |
| A | HOH2582 |
| B | LYS510 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD A 1521 |
| Chain | Residue |
| A | LEU275 |
| A | GLN279 |
| A | HOH2583 |
| A | HOH2584 |
| A | HOH2585 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD A 1522 |
| Chain | Residue |
| A | PHE6 |
| A | TYR144 |
| A | ALA148 |
| A | HOH2262 |
| A | HOH2586 |
| A | HOH2587 |
| A | HOH2588 |
| B | GLU158 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 1523 |
| Chain | Residue |
| A | ARG151 |
| A | TYR171 |
| A | HOH2269 |
| A | HOH2555 |
| A | HOH2589 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 1524 |
| Chain | Residue |
| A | ARG36 |
| A | PRO39 |
| A | HOH2309 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1525 |
| Chain | Residue |
| A | SER55 |
| A | LEU56 |
| A | GLU123 |
| A | ASP211 |
| A | HOH2143 |
| A | HOH2426 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GLY B 1517 |
| Chain | Residue |
| B | SER323 |
| B | GLY477 |
| B | ALA478 |
| B | PHE485 |
| B | HOH2236 |
| B | HOH2377 |
| B | HOH2515 |
| B | HOH2556 |
| site_id | BC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD B 1518 |
| Chain | Residue |
| B | GLY244 |
| B | ALA245 |
| B | PHE258 |
| B | THR259 |
| B | GLY260 |
| B | SER261 |
| B | VAL264 |
| B | GLU288 |
| B | THR289 |
| B | GLY290 |
| B | CYS322 |
| B | GLU417 |
| B | PHE419 |
| B | LEU445 |
| B | PHE485 |
| B | ACT1519 |
| B | HOH2557 |
| B | HOH2558 |
| B | HOH2559 |
| B | HOH2560 |
| B | HOH2561 |
| B | HOH2562 |
| B | HOH2563 |
| B | ILE180 |
| B | ALA181 |
| B | PRO182 |
| B | TRP183 |
| B | ASN184 |
| B | ILE189 |
| B | LYS207 |
| B | ALA209 |
| B | GLU210 |
| B | GLY240 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 1519 |
| Chain | Residue |
| B | ALA245 |
| B | GLU249 |
| B | ILE268 |
| B | ALA271 |
| B | NAD1518 |
| B | HOH2564 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 1520 |
| Chain | Residue |
| A | LYS510 |
| B | ARG462 |
| B | PHE464 |
| B | HIS465 |
| B | HOH2565 |
| B | HOH2566 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD B 1521 |
| Chain | Residue |
| B | ARG151 |
| B | HOH2540 |
| site_id | BC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MRD B 1522 |
| Chain | Residue |
| A | GLU158 |
| A | VAL160 |
| B | PHE6 |
| B | TYR144 |
| B | ALA148 |
| B | LEU500 |
| B | HOH2245 |
| B | HOH2567 |
| B | HOH2568 |
| B | HOH2569 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MRD B 1523 |
| Chain | Residue |
| B | LEU275 |
| B | GLN279 |
| B | HOH2570 |
| B | HOH2571 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD B 1524 |
| Chain | Residue |
| B | TYR38 |
| B | TRP46 |
| B | GLU221 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD B 1525 |
| Chain | Residue |
| A | LEU27 |
| A | ARG28 |
| A | TYR122 |
| A | GLU355 |
| B | PRO353 |
| B | GLU355 |
| B | GLU356 |
| B | HOH2573 |
| B | HOH2574 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 1526 |
| Chain | Residue |
| B | SER55 |
| B | LEU56 |
| B | GLU123 |
| B | ASP211 |
| B | HOH2132 |
| B | HOH2420 |
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 | 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 |
