2J40
1-pyrroline-5-carboxylate dehydrogenase from Thermus thermophilus with bound inhibitor L-proline 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 | 9 |
| Details | BINDING SITE FOR RESIDUE PRO A1517 |
| Chain | Residue |
| A | GLU137 |
| A | CSO322 |
| A | SER323 |
| A | GLY477 |
| A | ALA478 |
| A | PHE485 |
| A | HOH2376 |
| A | HOH2381 |
| A | HOH2405 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD A1518 |
| 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 | CSO322 |
| A | GLU417 |
| A | PHE419 |
| A | PHE485 |
| A | ACT1519 |
| A | HOH2406 |
| A | HOH2407 |
| A | HOH2408 |
| A | HOH2409 |
| A | HOH2410 |
| A | HOH2411 |
| A | HOH2412 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A1519 |
| Chain | Residue |
| A | ALA245 |
| A | GLU249 |
| A | ILE268 |
| A | ALA271 |
| A | NAD1518 |
| A | HOH2413 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A1520 |
| Chain | Residue |
| A | ARG462 |
| A | PHE464 |
| A | HIS465 |
| A | HOH2414 |
| B | LYS510 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A1522 |
| Chain | Residue |
| A | SER55 |
| A | LEU56 |
| A | GLU123 |
| A | ASP211 |
| A | HOH2199 |
| A | HOH2293 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PRO B1518 |
| Chain | Residue |
| B | GLU137 |
| B | PHE185 |
| B | CSO322 |
| B | SER323 |
| B | GLY477 |
| B | ALA478 |
| B | PHE485 |
| B | HOH2322 |
| B | HOH2361 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD B1519 |
| Chain | Residue |
| 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 |
| B | THR289 |
| B | GLY290 |
| B | CSO322 |
| B | GLU417 |
| B | PHE419 |
| B | PHE485 |
| B | ACT1520 |
| B | HOH2362 |
| B | HOH2363 |
| B | HOH2364 |
| B | HOH2365 |
| B | HOH2367 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B1520 |
| Chain | Residue |
| B | NAD1519 |
| B | ALA245 |
| B | GLU249 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B1521 |
| Chain | Residue |
| A | LYS510 |
| B | ARG462 |
| B | PHE464 |
| B | HIS465 |
| B | HOH2368 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B1526 |
| Chain | Residue |
| B | SER55 |
| B | LEU56 |
| B | GLU123 |
| B | ASP211 |
| B | HOH2071 |
| B | HOH2259 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MRD A1521 |
| Chain | Residue |
| A | HOH2415 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD B1525 |
| Chain | Residue |
| B | GLY278 |
| B | GLN279 |
| B | THR280 |
| B | HOH2372 |
| B | HOH2373 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD B1517 |
| Chain | Residue |
| A | GLU158 |
| B | PHE6 |
| B | TYR144 |
| B | ARG147 |
| B | ALA148 |
| B | HOH2358 |
| B | HOH2359 |
| B | HOH2360 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD B1522 |
| Chain | Residue |
| A | TYR144 |
| A | ALA148 |
| A | LEU500 |
| A | HOH2163 |
| B | GLU158 |
| B | HOH2369 |
| B | HOH2370 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B1523 |
| Chain | Residue |
| B | ARG36 |
| B | TYR38 |
| B | GLU221 |
| B | HOH2178 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD B1524 |
| Chain | Residue |
| A | LEU27 |
| A | ARG28 |
| A | TYR122 |
| A | GLU355 |
| B | PRO353 |
| B | GLU355 |
| B | GLU356 |
| B | HOH2371 |
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 |
