2EJD
Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from Thermus thermophilus with bound L-alanine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
A | 0010133 | biological_process | proline catabolic process to 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 | 1-pyrroline-5-carboxylate dehydrogenase activity |
B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
B | 0010133 | biological_process | proline catabolic process to 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 | HOH2578 |
A | SER55 |
A | LEU56 |
A | GLU123 |
A | ASP211 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 2520 |
Chain | Residue |
A | LYS510 |
B | ARG462 |
B | PHE464 |
B | HIS465 |
B | HOH2789 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 2540 |
Chain | Residue |
B | SER55 |
B | LEU56 |
B | GLU123 |
B | ASP211 |
B | HOH2788 |
B | HOH2923 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ALA 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 | HOH2993 |
A | HOH2994 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ALA B 2517 |
Chain | Residue |
B | PHE185 |
B | CSO322 |
B | SER323 |
B | THR476 |
B | GLY477 |
B | ALA478 |
B | PHE485 |
B | HOH2549 |
B | HOH2661 |
B | HOH2796 |
B | HOH2853 |
B | HOH2911 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD A 1530 |
Chain | Residue |
A | PHE6 |
A | TYR144 |
A | ALA148 |
A | HOH2573 |
A | HOH2574 |
A | HOH2612 |
A | HOH2924 |
B | GLU158 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD A 1531 |
Chain | Residue |
A | VAL312 |
A | ASP359 |
A | HOH2576 |
A | HOH2934 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD A 1532 |
Chain | Residue |
A | GLU241 |
A | GLY244 |
A | ALA245 |
A | HOH2577 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 1533 |
Chain | Residue |
A | TYR375 |
A | ARG412 |
A | HOH2927 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD B 1534 |
Chain | Residue |
B | GLN279 |
B | HOH2571 |
B | HOH2887 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 1535 |
Chain | Residue |
A | GLN279 |
A | HOH2793 |
B | PRO442 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD A 2530 |
Chain | Residue |
A | GLU158 |
A | VAL160 |
A | HOH2579 |
A | HOH2669 |
B | TYR144 |
B | ARG147 |
B | ALA148 |
B | HOH2785 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD A 2531 |
Chain | Residue |
A | ARG151 |
A | LEU500 |
A | HOH2983 |
B | MPD2532 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD B 2532 |
Chain | Residue |
A | MPD2531 |
B | ARG151 |
B | HOH2918 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD B 2534 |
Chain | Residue |
B | GLU241 |
B | ALA245 |
B | HOH2648 |
B | HOH2895 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD B 2535 |
Chain | Residue |
A | ARG24 |
A | LEU27 |
A | TYR122 |
A | GLU355 |
B | PRO353 |
B | GLU355 |
B | GLU356 |
B | HOH2725 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD B 2536 |
Chain | Residue |
B | GLY316 |
B | ASP359 |
B | HOH2620 |
B | VAL312 |
B | TYR315 |
site_id | CC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MPD B 2537 |
Chain | Residue |
B | ARG36 |
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 |