4I26
2.20 Angstroms X-ray crystal structure of 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 | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 601 |
| Chain | Residue |
| A | ARG120 |
| A | LEU174 |
| A | TYR462 |
| A | ARG464 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 601 |
| Chain | Residue |
| B | ARG120 |
| B | LEU174 |
| B | TYR462 |
| B | ARG464 |
| B | PHE470 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 602 |
| Chain | Residue |
| A | GLU264 |
| A | VAL265 |
| A | LEU478 |
| B | GLU264 |
| B | VAL265 |
| B | LEU478 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 603 |
| Chain | Residue |
| B | ASP488 |
| B | SER491 |
| B | HOH749 |
| B | HOH766 |
| B | HOH835 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 601 |
| Chain | Residue |
| C | ARG120 |
| C | LEU174 |
| C | TYR462 |
| C | ARG464 |
| C | PHE470 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 602 |
| Chain | Residue |
| C | ASP488 |
| C | PHE489 |
| C | SER491 |
| C | HOH728 |
| C | HOH729 |
| C | HOH841 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 601 |
| Chain | Residue |
| D | ARG120 |
| D | LEU174 |
| D | TYR462 |
| D | ARG464 |
| D | PHE470 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 602 |
| Chain | Residue |
| D | ASP488 |
| D | PHE489 |
| D | SER491 |
| D | HOH839 |
| D | HOH853 |
| D | HOH861 |
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 |
