4NPI
1.94 Angstroms X-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-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 | 26 |
| Details | BINDING SITE FOR RESIDUE NAD A 601 |
| Chain | Residue |
| A | ILE165 |
| A | GLY225 |
| A | GLY230 |
| A | GLU231 |
| A | PHE244 |
| A | GLY246 |
| A | GLU247 |
| A | THR250 |
| A | GLU268 |
| A | LEU269 |
| A | GLY270 |
| A | SER166 |
| A | CYS302 |
| A | LYS352 |
| A | GLU404 |
| A | PHE406 |
| A | 2VS603 |
| A | HOH1102 |
| A | HOH1109 |
| A | PRO167 |
| A | TRP168 |
| A | ASN169 |
| A | LYS192 |
| A | SER194 |
| A | GLU195 |
| A | PHE224 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 602 |
| Chain | Residue |
| A | ASN37 |
| A | ILE38 |
| A | ASP105 |
| A | GLU196 |
| A | HOH779 |
| A | HOH799 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 2VS A 603 |
| Chain | Residue |
| A | ARG120 |
| A | ASN169 |
| A | LEU170 |
| A | LEU174 |
| A | TRP177 |
| A | GLU268 |
| A | CYS302 |
| A | TYR462 |
| A | ARG464 |
| A | PHE470 |
| A | NAD601 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD B 601 |
| Chain | Residue |
| B | ILE165 |
| B | SER166 |
| B | PRO167 |
| B | TRP168 |
| B | ASN169 |
| 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 | GLU268 |
| B | GLY270 |
| B | CYS302 |
| B | LYS352 |
| B | GLU404 |
| B | PHE406 |
| B | 2VS603 |
| B | HOH740 |
| B | HOH817 |
| B | HOH870 |
| B | HOH919 |
| B | HOH1026 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 602 |
| Chain | Residue |
| B | ASN37 |
| B | ILE38 |
| B | ASP105 |
| B | GLU196 |
| B | HOH755 |
| B | HOH810 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 2VS B 603 |
| Chain | Residue |
| B | ARG120 |
| B | ASN169 |
| B | LEU174 |
| B | TRP177 |
| B | GLU268 |
| B | VAL301 |
| B | CYS302 |
| B | TYR462 |
| B | ARG464 |
| B | PHE470 |
| B | NAD601 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD C 601 |
| Chain | Residue |
| C | GLY225 |
| C | GLY230 |
| C | GLU231 |
| C | PHE244 |
| C | GLY246 |
| C | GLU247 |
| C | THR250 |
| C | THR253 |
| C | GLU268 |
| C | LEU269 |
| C | GLY270 |
| C | CYS302 |
| C | LYS352 |
| C | GLU404 |
| C | PHE406 |
| C | 2VS603 |
| C | HOH904 |
| C | HOH1009 |
| C | ILE165 |
| C | SER166 |
| C | PRO167 |
| C | TRP168 |
| C | ASN169 |
| C | LYS192 |
| C | SER194 |
| C | GLU195 |
| C | PHE224 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 602 |
| Chain | Residue |
| C | ASN37 |
| C | ILE38 |
| C | ASP105 |
| C | GLU196 |
| C | HOH996 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 2VS C 603 |
| Chain | Residue |
| C | ARG120 |
| C | ASN169 |
| C | LEU170 |
| C | LEU174 |
| C | TRP177 |
| C | GLU268 |
| C | CYS302 |
| C | TYR462 |
| C | ARG464 |
| C | PHE470 |
| C | NAD601 |
| C | HOH827 |
| site_id | BC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD D 601 |
| Chain | Residue |
| D | ILE165 |
| D | SER166 |
| D | PRO167 |
| D | TRP168 |
| D | LYS192 |
| D | SER194 |
| D | GLU195 |
| D | PHE224 |
| 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 | HIS349 |
| D | LYS352 |
| D | GLU404 |
| D | PHE406 |
| D | 2VS603 |
| D | HOH810 |
| D | HOH969 |
| D | HOH974 |
| D | HOH1002 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 602 |
| Chain | Residue |
| D | ASN37 |
| D | ILE38 |
| D | ASP105 |
| D | GLU196 |
| D | HOH783 |
| D | HOH1005 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 2VS D 603 |
| Chain | Residue |
| D | ARG120 |
| D | ASN169 |
| D | LEU170 |
| D | LEU174 |
| D | GLU268 |
| D | CYS302 |
| D | TYR462 |
| D | ARG464 |
| D | PHE470 |
| D | NAD601 |
| D | HOH789 |
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 |
