2EIT
Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from Thermus thermophilus with bound L-alanine 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 1519 |
| Chain | Residue |
| A | GLU249 |
| A | ILE268 |
| A | ALA271 |
| A | NAD1518 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 1520 |
| Chain | Residue |
| B | LYS510 |
| A | ARG462 |
| A | PHE464 |
| A | HIS465 |
| A | HOH2755 |
| A | HOH2970 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1521 |
| Chain | Residue |
| A | SER55 |
| A | LEU56 |
| A | GLU123 |
| A | ASP211 |
| A | HOH2612 |
| A | HOH2692 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 2519 |
| Chain | Residue |
| B | ALA245 |
| B | GLU249 |
| B | LYS267 |
| B | ILE268 |
| B | ALA271 |
| B | NAD2518 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 2520 |
| Chain | Residue |
| A | LYS510 |
| B | ARG462 |
| B | PHE464 |
| B | HIS465 |
| B | HOH2773 |
| B | HOH2920 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 2521 |
| Chain | Residue |
| B | SER55 |
| B | LEU56 |
| B | GLU123 |
| B | ASP211 |
| B | HOH2601 |
| B | HOH2812 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ALA A 1517 |
| Chain | Residue |
| A | CYS322 |
| A | SER323 |
| A | GLY477 |
| A | ALA478 |
| A | PHE485 |
| A | HOH2543 |
| A | HOH2592 |
| A | HOH2789 |
| A | HOH2839 |
| A | HOH2997 |
| site_id | AC8 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD A 1518 |
| Chain | Residue |
| A | ILE180 |
| A | ALA181 |
| A | PRO182 |
| A | TRP183 |
| A | ASN184 |
| A | ILE189 |
| A | LYS207 |
| A | ALA209 |
| A | GLU210 |
| A | GLY240 |
| 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 | HOH2723 |
| A | HOH2772 |
| A | HOH2792 |
| A | HOH2997 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ALA B 2517 |
| Chain | Residue |
| B | CYS322 |
| B | SER323 |
| B | GLY477 |
| B | ALA478 |
| B | PHE485 |
| B | HOH2543 |
| B | HOH2623 |
| B | HOH2907 |
| site_id | BC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 2518 |
| Chain | Residue |
| B | THR289 |
| B | GLY290 |
| B | CYS322 |
| B | GLU417 |
| B | PHE419 |
| B | PHE485 |
| B | ACT2519 |
| B | HOH2704 |
| B | HOH2723 |
| B | HOH2765 |
| B | HOH2922 |
| B | HOH2972 |
| B | HOH2974 |
| B | ILE180 |
| B | ALA181 |
| B | PRO182 |
| B | TRP183 |
| B | ASN184 |
| B | ILE189 |
| B | LYS207 |
| B | ALA209 |
| B | GLU210 |
| B | GLY240 |
| B | GLY244 |
| B | ALA245 |
| B | PHE258 |
| B | THR259 |
| B | GLY260 |
| B | SER261 |
| B | VAL264 |
| B | GLU288 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD A 1530 |
| Chain | Residue |
| A | GLU158 |
| A | HOH2628 |
| A | HOH2663 |
| A | HOH2875 |
| B | PHE6 |
| B | TYR144 |
| B | ALA148 |
| B | HOH2580 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD A 1531 |
| Chain | Residue |
| A | ASP359 |
| A | HOH2623 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 1533 |
| Chain | Residue |
| A | ARG151 |
| A | TYR152 |
| A | LEU500 |
| A | HOH2863 |
| A | HOH2864 |
| B | MPD2534 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MPD A 2530 |
| Chain | Residue |
| A | PHE6 |
| A | TYR144 |
| A | ALA148 |
| A | LEU500 |
| A | HOH2593 |
| A | HOH2621 |
| A | HOH2670 |
| B | GLU158 |
| B | VAL160 |
| B | HOH2852 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 2531 |
| Chain | Residue |
| B | ARG36 |
| B | GLU221 |
| B | HOH2745 |
| B | HOH2909 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD B 2532 |
| Chain | Residue |
| A | LEU27 |
| A | ARG28 |
| A | TYR122 |
| A | GLU355 |
| B | PRO353 |
| B | GLU355 |
| B | GLU356 |
| B | HOH2687 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD B 2533 |
| Chain | Residue |
| B | GLN279 |
| B | HOH2631 |
| B | HOH2822 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 2534 |
| Chain | Residue |
| A | MPD1533 |
| B | TYR171 |
| B | HOH2827 |
| B | HOH2908 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 2535 |
| Chain | Residue |
| A | LEU275 |
| A | GLN279 |
| A | HOH2708 |
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 |
