4I1W
2.00 Angstroms X-ray crystal structure of NAD- bound 2-aminomuconate 6-semialdehyde dehydrogenase from Pseudomonas fluorescens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 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 | 32 |
| Details | BINDING SITE FOR RESIDUE NAD A 601 |
| Chain | Residue |
| A | ILE165 |
| A | PHE224 |
| A | GLY225 |
| A | LYS226 |
| A | GLY230 |
| A | GLU231 |
| A | PHE244 |
| A | THR245 |
| A | GLY246 |
| A | GLU247 |
| A | THR250 |
| A | SER166 |
| A | GLU268 |
| A | LEU269 |
| A | GLY270 |
| A | CYS302 |
| A | GLU404 |
| A | PHE406 |
| A | PHE470 |
| A | HOH867 |
| A | HOH884 |
| A | HOH966 |
| A | PRO167 |
| A | HOH1009 |
| A | HOH1080 |
| A | HOH1110 |
| A | TRP168 |
| A | ASN169 |
| A | LEU174 |
| A | LYS192 |
| A | SER194 |
| A | GLU195 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B 601 |
| Chain | Residue |
| B | ILE165 |
| B | SER166 |
| B | PRO167 |
| B | TRP168 |
| B | ASN169 |
| B | LEU174 |
| B | LYS192 |
| B | SER194 |
| B | GLU195 |
| B | PHE224 |
| B | GLY225 |
| B | LYS226 |
| B | GLY230 |
| B | GLU231 |
| B | PHE244 |
| B | THR245 |
| B | GLY246 |
| B | GLU247 |
| B | THR250 |
| B | THR253 |
| B | GLU268 |
| B | LEU269 |
| B | GLY270 |
| B | CYS302 |
| B | GLU404 |
| B | PHE406 |
| B | PHE470 |
| B | HOH779 |
| B | HOH785 |
| B | HOH969 |
| B | HOH990 |
| B | HOH1082 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD C 601 |
| Chain | Residue |
| C | ILE165 |
| C | SER166 |
| C | PRO167 |
| C | TRP168 |
| C | ASN169 |
| C | LEU174 |
| C | LYS192 |
| C | SER194 |
| C | GLU195 |
| C | PHE224 |
| C | GLY225 |
| C | LYS226 |
| C | GLY230 |
| C | GLU231 |
| C | PHE244 |
| C | THR245 |
| C | GLY246 |
| C | GLU247 |
| C | THR250 |
| C | GLU268 |
| C | LEU269 |
| C | GLY270 |
| C | CYS302 |
| C | GLU404 |
| C | PHE406 |
| C | PHE470 |
| C | HOH807 |
| C | HOH822 |
| C | HOH922 |
| C | HOH1049 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 602 |
| Chain | Residue |
| C | PHE470 |
| C | ARG120 |
| C | LEU174 |
| C | TRP177 |
| C | TYR462 |
| C | ARG464 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD D 601 |
| Chain | Residue |
| D | ILE165 |
| D | SER166 |
| D | PRO167 |
| D | TRP168 |
| D | ASN169 |
| D | LEU174 |
| D | LYS192 |
| D | SER194 |
| D | GLU195 |
| D | GLY225 |
| D | LYS226 |
| D | GLY230 |
| D | GLU231 |
| D | PHE244 |
| D | THR245 |
| D | GLY246 |
| D | GLU247 |
| D | THR250 |
| D | GLU268 |
| D | LEU269 |
| D | GLY270 |
| D | CYS302 |
| D | GLU404 |
| D | PHE406 |
| D | PHE470 |
| D | HOH765 |
| D | HOH783 |
| D | HOH979 |
| D | HOH1071 |
| D | HOH1120 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 602 |
| Chain | Residue |
| D | ARG120 |
| D | TRP177 |
| D | TYR462 |
| D | ARG464 |
| D | PHE470 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FtNSGQVCLCSE |
| Chain | Residue | Details |
| A | PHE295-GLU306 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. FELGGKNA |
| Chain | Residue | Details |
| A | PHE267-ALA274 |
