2IY6
1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS WITH BOUND CITRATE
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 | 16 |
| Details | BINDING SITE FOR RESIDUE FLC A1517 |
| Chain | Residue |
| A | GLU137 |
| A | HOH2240 |
| A | HOH2542 |
| A | HOH2546 |
| A | HOH2577 |
| A | HOH2578 |
| A | HOH2579 |
| A | HOH2581 |
| A | ASN184 |
| A | PHE185 |
| A | LYS321 |
| A | CYS322 |
| A | SER323 |
| A | GLY477 |
| A | ALA478 |
| A | PHE485 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A1540 |
| Chain | Residue |
| A | SER55 |
| A | LEU56 |
| A | GLU123 |
| A | ASP211 |
| A | HOH2130 |
| A | HOH2219 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A1541 |
| Chain | Residue |
| A | LYS510 |
| B | HIS465 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FLC B1517 |
| Chain | Residue |
| B | GLU137 |
| B | ASN184 |
| B | PHE185 |
| B | LYS321 |
| B | CYS322 |
| B | SER323 |
| B | GLY477 |
| B | ALA478 |
| B | PHE485 |
| B | HOH2218 |
| B | HOH2351 |
| B | HOH2507 |
| B | HOH2518 |
| B | HOH2553 |
| B | HOH2554 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B1540 |
| Chain | Residue |
| B | SER55 |
| B | LEU56 |
| B | GLU123 |
| B | ASP211 |
| B | HOH2116 |
| B | HOH2409 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B1541 |
| Chain | Residue |
| A | HIS465 |
| B | LYS510 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD A1532 |
| Chain | Residue |
| A | LEU275 |
| A | GLN279 |
| A | HOH2585 |
| A | HOH2586 |
| A | HOH2587 |
| B | MPD1531 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MRD A1533 |
| Chain | Residue |
| A | GLU241 |
| A | GLY244 |
| A | ALA245 |
| A | HOH2318 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MRD B1534 |
| Chain | Residue |
| B | GLN279 |
| B | MPD1533 |
| B | HOH2563 |
| B | HOH2564 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD B1535 |
| Chain | Residue |
| B | ILE180 |
| B | GLU241 |
| B | GLY244 |
| B | ALA245 |
| B | HOH2306 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD B1537 |
| Chain | Residue |
| B | PRO5 |
| B | ARG110 |
| B | GLU143 |
| B | HOH2228 |
| B | HOH2566 |
| B | HOH2567 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD A1530 |
| Chain | Residue |
| A | GLU158 |
| A | HOH2582 |
| A | HOH2583 |
| A | HOH2584 |
| B | PHE6 |
| B | TYR144 |
| B | ARG147 |
| B | ALA148 |
| B | HOH2229 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A1531 |
| Chain | Residue |
| A | VAL311 |
| A | VAL312 |
| A | ASP359 |
| A | HOH2232 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A1534 |
| Chain | Residue |
| A | ARG151 |
| A | HOH2588 |
| A | HOH2589 |
| A | HOH2590 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD B1530 |
| Chain | Residue |
| A | PHE6 |
| A | TYR144 |
| A | ARG147 |
| A | ALA148 |
| A | HOH2248 |
| B | GLU158 |
| B | HOH2555 |
| B | HOH2556 |
| B | HOH2557 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD B1531 |
| Chain | Residue |
| B | GLU416 |
| B | HOH2324 |
| B | HOH2558 |
| B | HOH2559 |
| A | MRD1532 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD B1532 |
| Chain | Residue |
| A | LEU27 |
| A | TYR122 |
| A | GLU355 |
| B | PRO353 |
| B | GLU355 |
| B | GLU356 |
| B | HOH2560 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B1533 |
| Chain | Residue |
| A | GLU416 |
| B | MRD1534 |
| B | HOH2561 |
| B | HOH2562 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD B1536 |
| Chain | Residue |
| A | HOH2588 |
| B | ARG151 |
| B | TYR171 |
| B | HOH2533 |
| B | HOH2565 |
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 |
