2EHQ
Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NADP
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 1519 |
| Chain | Residue |
| A | ALA245 |
| A | GLU249 |
| A | ILE268 |
| A | ALA271 |
| A | NAP1518 |
| A | HOH2034 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 1520 |
| Chain | Residue |
| A | HOH1808 |
| B | LYS510 |
| A | ARG462 |
| A | PHE464 |
| A | HIS465 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1540 |
| Chain | Residue |
| A | SER55 |
| A | LEU56 |
| A | GLU123 |
| A | ASP211 |
| A | HOH1716 |
| A | HOH1851 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 2519 |
| Chain | Residue |
| B | ALA245 |
| B | GLU249 |
| B | ILE268 |
| B | ALA271 |
| B | NAP2518 |
| B | HOH3040 |
| 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 | HOH2810 |
| B | HOH2990 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 2540 |
| Chain | Residue |
| B | SER55 |
| B | LEU56 |
| B | GLU123 |
| B | ASP211 |
| B | HOH2790 |
| B | HOH3019 |
| site_id | AC7 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NAP A 1518 |
| Chain | Residue |
| A | ILE180 |
| A | ALA181 |
| A | PRO182 |
| A | TRP183 |
| A | ASN184 |
| A | ILE189 |
| A | LYS207 |
| A | ALA209 |
| A | GLU210 |
| A | GLY238 |
| A | VAL239 |
| A | GLY240 |
| A | GLU241 |
| 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 | HOH1612 |
| A | HOH1627 |
| A | HOH1633 |
| A | HOH1822 |
| A | HOH1848 |
| A | HOH1940 |
| A | HOH2009 |
| A | HOH2078 |
| A | HOH2080 |
| site_id | AC8 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE NAP B 2518 |
| Chain | Residue |
| B | ACT2519 |
| B | HOH2602 |
| B | HOH2641 |
| B | HOH2659 |
| B | HOH2823 |
| B | HOH2874 |
| B | HOH2896 |
| B | HOH2991 |
| B | HOH3002 |
| B | HOH3022 |
| B | HOH3042 |
| B | ILE180 |
| B | ALA181 |
| B | PRO182 |
| B | TRP183 |
| B | ASN184 |
| B | ILE189 |
| B | LYS207 |
| B | ALA209 |
| B | GLU210 |
| B | GLY238 |
| B | VAL239 |
| B | GLY240 |
| B | GLY244 |
| B | ALA245 |
| B | PHE258 |
| B | THR259 |
| B | GLY260 |
| B | SER261 |
| B | VAL264 |
| B | GLU288 |
| B | THR289 |
| B | GLY290 |
| B | CYS322 |
| B | GLU417 |
| B | PHE419 |
| B | LEU445 |
| B | PHE485 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 1531 |
| Chain | Residue |
| A | LEU275 |
| A | GLN279 |
| A | HOH1654 |
| A | HOH1934 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 1533 |
| Chain | Residue |
| A | ARG151 |
| A | TYR171 |
| A | HOH1871 |
| A | HOH1921 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD A 1534 |
| Chain | Residue |
| A | ASP359 |
| A | HOH1670 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD B 2531 |
| Chain | Residue |
| B | ARG151 |
| B | HOH2981 |
| B | HOH3041 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD B 2532 |
| Chain | Residue |
| A | GLU158 |
| A | VAL160 |
| B | PHE6 |
| B | TYR144 |
| B | ALA148 |
| B | HOH2574 |
| B | HOH2610 |
| B | HOH2656 |
| B | HOH2941 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 2533 |
| Chain | Residue |
| B | LEU275 |
| B | GLN279 |
| B | HOH2645 |
| B | HOH2934 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD B 2535 |
| Chain | Residue |
| A | LEU27 |
| A | TYR122 |
| A | GLU355 |
| B | PRO353 |
| B | GLU355 |
| B | GLU356 |
| B | HOH2664 |
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 |
