2EIW
Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from Thermus thermophilus with bound L-proline
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 | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 1520 |
| Chain | Residue |
| A | ARG462 |
| A | PHE464 |
| A | HIS465 |
| A | HOH5833 |
| B | VAL172 |
| B | LYS510 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1540 |
| Chain | Residue |
| A | ASP211 |
| A | HOH5703 |
| A | HOH5916 |
| A | SER55 |
| A | LEU56 |
| A | GLU123 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 5520 |
| Chain | Residue |
| A | LYS510 |
| B | ARG462 |
| B | PHE464 |
| B | HIS465 |
| B | HOH5719 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 5540 |
| Chain | Residue |
| B | SER55 |
| B | LEU56 |
| B | GLU123 |
| B | ASP211 |
| B | HOH5892 |
| B | HOH5893 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PRO A 5517 |
| Chain | Residue |
| A | GLU137 |
| A | PHE185 |
| A | SER323 |
| A | GLY477 |
| A | ALA478 |
| A | PHE485 |
| A | HOH5552 |
| A | HOH5666 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PRO B 5541 |
| Chain | Residue |
| B | GLU137 |
| B | PHE185 |
| B | SER323 |
| B | GLY477 |
| B | ALA478 |
| B | PHE485 |
| B | HOH5548 |
| B | HOH5657 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 1530 |
| Chain | Residue |
| A | ALA148 |
| A | HOH5595 |
| B | GLU158 |
| B | VAL160 |
| B | HOH5622 |
| B | HOH5644 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD A 1531 |
| Chain | Residue |
| A | ASP359 |
| A | HOH5635 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 1532 |
| Chain | Residue |
| A | GLU241 |
| A | GLY244 |
| A | ALA245 |
| A | HOH5765 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 1533 |
| Chain | Residue |
| A | GLU416 |
| A | HOH5574 |
| A | HOH5669 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD A 5530 |
| Chain | Residue |
| A | GLU158 |
| A | HOH5602 |
| A | HOH5706 |
| B | PHE6 |
| B | TYR144 |
| B | ALA148 |
| B | HOH5616 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MPD A 5531 |
| Chain | Residue |
| A | ARG151 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 5532 |
| Chain | Residue |
| A | HOH5777 |
| B | ARG151 |
| B | TYR171 |
| B | LEU500 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 5534 |
| Chain | Residue |
| B | GLU241 |
| B | GLY244 |
| B | ALA245 |
| B | VAL264 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD B 5535 |
| Chain | Residue |
| A | ARG28 |
| A | TYR122 |
| A | GLU355 |
| B | PRO353 |
| B | GLU355 |
| B | GLU356 |
| B | HOH5704 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD B 5536 |
| Chain | Residue |
| B | TYR315 |
| B | ASP359 |
| B | HOH5639 |
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 |
