5J6B
Crystal structure of Aldehyde dehydrogenase from Burkholderia thailandensis in covelent complex with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
| 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 | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
| 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 | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
| 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 | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
| 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 | 3 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | PRO130 |
| A | ARG131 |
| A | HOH1687 |
| site_id | AC2 |
| Number of Residues | 34 |
| Details | binding site for residue NDP A 502 |
| Chain | Residue |
| A | LYS177 |
| A | PRO178 |
| A | ALA179 |
| A | SER180 |
| A | ARG181 |
| A | ALA208 |
| A | ARG210 |
| A | ALA213 |
| A | PHE227 |
| A | THR228 |
| A | GLY229 |
| A | SER230 |
| A | PRO231 |
| A | VAL233 |
| A | LEU237 |
| A | GLU249 |
| A | LEU250 |
| A | GLY251 |
| A | CYS285 |
| A | GLU379 |
| A | PHE381 |
| A | TYR446 |
| A | HOH1311 |
| A | HOH1332 |
| A | HOH1338 |
| A | HOH1364 |
| A | HOH1378 |
| A | HOH1404 |
| A | ILE150 |
| A | SER151 |
| A | PRO152 |
| A | PHE153 |
| A | ASN154 |
| A | LEU159 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 501 |
| Chain | Residue |
| B | SER129 |
| B | PRO130 |
| B | ARG131 |
| B | HOH797 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 501 |
| Chain | Residue |
| C | SER129 |
| C | PRO130 |
| C | ARG131 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 501 |
| Chain | Residue |
| D | PRO130 |
| D | ARG131 |
| site_id | AC6 |
| Number of Residues | 37 |
| Details | binding site for Di-peptide NDP B 502 and CYS B 285 |
| Chain | Residue |
| B | ILE150 |
| B | SER151 |
| B | PRO152 |
| B | PHE153 |
| B | ASN154 |
| B | LEU159 |
| B | LYS177 |
| B | ALA179 |
| B | SER180 |
| B | ARG181 |
| B | ALA208 |
| B | ARG210 |
| B | ALA213 |
| B | PHE227 |
| B | THR228 |
| B | GLY229 |
| B | SER230 |
| B | PRO231 |
| B | VAL233 |
| B | GLU249 |
| B | LEU250 |
| B | GLY251 |
| B | SER284 |
| B | ILE286 |
| B | GLY287 |
| B | GLU379 |
| B | PHE381 |
| B | LEU407 |
| B | TYR446 |
| B | HOH610 |
| B | HOH611 |
| B | HOH620 |
| B | HOH626 |
| B | HOH639 |
| B | HOH673 |
| B | HOH688 |
| B | HOH778 |
| site_id | AC7 |
| Number of Residues | 36 |
| Details | binding site for Di-peptide NDP C 502 and CYS C 285 |
| Chain | Residue |
| C | SER230 |
| C | PRO231 |
| C | VAL233 |
| C | GLU249 |
| C | LEU250 |
| C | GLY251 |
| C | SER284 |
| C | ILE286 |
| C | GLY287 |
| C | GLU379 |
| C | PHE381 |
| C | LEU407 |
| C | TYR446 |
| C | HOH609 |
| C | HOH621 |
| C | HOH645 |
| C | HOH656 |
| C | HOH663 |
| C | HOH667 |
| C | HOH815 |
| C | ILE150 |
| C | SER151 |
| C | PRO152 |
| C | PHE153 |
| C | ASN154 |
| C | LEU159 |
| C | LYS177 |
| C | ALA179 |
| C | SER180 |
| C | ARG181 |
| C | ALA208 |
| C | ARG210 |
| C | ALA213 |
| C | PHE227 |
| C | THR228 |
| C | GLY229 |
| site_id | AC8 |
| Number of Residues | 40 |
| Details | binding site for Di-peptide NDP D 502 and CYS D 285 |
| Chain | Residue |
| D | ILE150 |
| D | SER151 |
| D | PRO152 |
| D | PHE153 |
| D | ASN154 |
| D | LEU159 |
| D | LYS177 |
| D | PRO178 |
| D | ALA179 |
| D | SER180 |
| D | ARG181 |
| D | ALA208 |
| D | ARG210 |
| D | ALA213 |
| D | PHE227 |
| D | THR228 |
| D | GLY229 |
| D | SER230 |
| D | PRO231 |
| D | VAL233 |
| D | GLU249 |
| D | LEU250 |
| D | GLY251 |
| D | SER284 |
| D | ILE286 |
| D | GLY287 |
| D | GLU379 |
| D | PHE381 |
| D | LEU407 |
| D | TYR446 |
| D | HOH619 |
| D | HOH631 |
| D | HOH645 |
| D | HOH646 |
| D | HOH656 |
| D | HOH687 |
| D | HOH705 |
| D | HOH782 |
| D | HOH825 |
| D | HOH835 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGNAA |
| Chain | Residue | Details |
| A | LEU248-ALA255 |
