5U0L
X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from Marinobacter aquaeolei VT8 complexed with a substrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006527 | biological_process | arginine catabolic process |
| 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 |
| A | 0019544 | biological_process | arginine catabolic process to glutamate |
| A | 0019545 | biological_process | arginine catabolic process to succinate |
| A | 0043824 | molecular_function | succinylglutamate-semialdehyde dehydrogenase activity |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006527 | biological_process | arginine catabolic process |
| 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 |
| B | 0019544 | biological_process | arginine catabolic process to glutamate |
| B | 0019545 | biological_process | arginine catabolic process to succinate |
| B | 0043824 | molecular_function | succinylglutamate-semialdehyde dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | PHE393 |
| A | ASP394 |
| A | ARG421 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | HOH622 |
| A | GLY147 |
| A | LYS173 |
| A | PRO174 |
| A | SER175 |
| A | GLU176 |
| A | EDO508 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | SER441 |
| A | SER442 |
| A | HOH608 |
| B | VAL128 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | HIS123 |
| A | ARG136 |
| A | ARG138 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | ASN252 |
| A | ARG287 |
| A | GLU376 |
| A | TYR388 |
| A | ASN402 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | PRO457 |
| A | TYR461 |
| A | ASP464 |
| B | ASP464 |
| B | PRO469 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue 8YP A 507 |
| Chain | Residue |
| A | LYS109 |
| A | HIS154 |
| A | LEU155 |
| A | GLY158 |
| A | HIS159 |
| A | THR224 |
| A | SER458 |
| A | ALA459 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | SER206 |
| A | EDO502 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | CYS282 |
| A | THR283 |
| A | THR438 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue MPD B 501 |
| Chain | Residue |
| B | GLN258 |
| B | PHE393 |
| B | ARG421 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 502 |
| Chain | Residue |
| A | HIS234 |
| A | ASN454 |
| A | ARG456 |
| B | LEU245 |
| B | ARG456 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | ARG138 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 504 |
| Chain | Residue |
| A | ASP359 |
| A | ARG416 |
| B | GLU125 |
| B | GLU474 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FlSAGQRCTCAR |
| Chain | Residue | Details |
| A | PHE275-ARG286 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LEMGGNNP |
| Chain | Residue | Details |
| A | LEU247-PRO254 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01174 |
| Chain | Residue | Details |
| A | GLU248 | |
| A | CYS282 | |
| B | GLU248 | |
| B | CYS282 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01174 |
| Chain | Residue | Details |
| A | GLY225 | |
| B | GLY225 |
