2EJL
Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from Thermus thermophilus with bound L-serine
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 | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 1520 |
| Chain | Residue |
| A | ARG462 |
| A | PHE464 |
| A | HIS465 |
| A | HOH2816 |
| B | LYS510 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1540 |
| Chain | Residue |
| A | HOH2577 |
| A | SER55 |
| A | LEU56 |
| A | GLU123 |
| A | ASP211 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 2520 |
| Chain | Residue |
| A | LYS510 |
| B | ARG462 |
| B | PHE464 |
| B | HIS465 |
| B | HOH2777 |
| B | HOH2975 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA B 2540 |
| Chain | Residue |
| B | SER55 |
| B | LEU56 |
| B | GLU123 |
| B | ASP211 |
| B | HOH2954 |
| B | HOH2984 |
| B | HOH2985 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SER A 1517 |
| Chain | Residue |
| A | PHE185 |
| A | CSO322 |
| A | SER323 |
| A | THR476 |
| A | GLY477 |
| A | ALA478 |
| A | PHE485 |
| A | HOH2536 |
| A | HOH2586 |
| A | HOH2812 |
| A | HOH2979 |
| A | HOH3062 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SER B 2517 |
| Chain | Residue |
| B | PHE185 |
| B | CSO322 |
| B | SER323 |
| B | GLY477 |
| B | ALA478 |
| B | PHE485 |
| B | HOH2549 |
| B | HOH2657 |
| B | HOH2783 |
| B | HOH2838 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD A 1530 |
| Chain | Residue |
| A | PHE6 |
| A | TYR144 |
| A | ARG147 |
| A | ALA148 |
| A | HOH2572 |
| A | HOH2573 |
| A | HOH2614 |
| A | HOH3053 |
| B | GLU158 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 1531 |
| Chain | Residue |
| A | VAL312 |
| A | ASP359 |
| A | HOH2575 |
| A | HOH2923 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 1532 |
| Chain | Residue |
| A | GLU241 |
| A | GLY244 |
| A | ALA245 |
| A | HOH2576 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 1533 |
| Chain | Residue |
| A | SER374 |
| A | TYR375 |
| A | ILE378 |
| A | HOH2918 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD B 1534 |
| Chain | Residue |
| B | GLN279 |
| B | HOH2572 |
| B | HOH2868 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 1535 |
| Chain | Residue |
| A | LEU275 |
| A | GLN279 |
| A | HOH2793 |
| A | HOH3015 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD A 2530 |
| Chain | Residue |
| A | GLU158 |
| A | HOH2578 |
| A | HOH2672 |
| A | HOH3021 |
| B | PHE6 |
| B | TYR144 |
| B | ARG147 |
| B | ALA148 |
| B | HOH2775 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 2531 |
| Chain | Residue |
| A | ARG151 |
| A | TYR152 |
| A | HOH2971 |
| A | HOH3017 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 2532 |
| Chain | Residue |
| B | ARG151 |
| B | TYR171 |
| B | HOH2894 |
| B | HOH2976 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 2534 |
| Chain | Residue |
| B | GLU241 |
| B | GLY244 |
| B | ALA245 |
| B | HOH2644 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD B 2535 |
| Chain | Residue |
| B | GLU355 |
| B | GLU356 |
| B | HOH2720 |
| B | HOH2914 |
| A | LEU27 |
| A | ARG28 |
| A | TYR122 |
| A | GLU355 |
| B | PRO353 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 2536 |
| Chain | Residue |
| B | VAL312 |
| B | TYR315 |
| B | GLY316 |
| B | LEU349 |
| B | ASP359 |
| B | HOH2618 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD B 2537 |
| Chain | Residue |
| B | ARG36 |
| B | TRP46 |
| B | GLU221 |
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 |
