5N5S
Crystal structure of aldehyde dehydrogenase 21 (ALDH21) from Physcomitrella patens in complex with NADP+
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 | 24 |
| Details | binding site for residue NAP A 600 |
| Chain | Residue |
| A | VAL167 |
| A | VAL226 |
| A | ARG228 |
| A | ALA231 |
| A | PHE245 |
| A | THR246 |
| A | GLY247 |
| A | SER248 |
| A | ILE251 |
| A | GLU267 |
| A | LEU268 |
| A | SER168 |
| A | GLY269 |
| A | CYS302 |
| A | GLU396 |
| A | PHE398 |
| A | TYR463 |
| A | PRO169 |
| A | TRP170 |
| A | ASN171 |
| A | LEU176 |
| A | LYS194 |
| A | ALA196 |
| A | SER197 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | ASP277 |
| B | ARG313 |
| B | LYS435 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | binding site for residue NAP B 502 |
| Chain | Residue |
| B | VAL167 |
| B | SER168 |
| B | PRO169 |
| B | TRP170 |
| B | ASN171 |
| B | LEU176 |
| B | LYS194 |
| B | ALA196 |
| B | SER197 |
| B | ARG198 |
| B | VAL226 |
| B | ARG228 |
| B | ALA231 |
| B | PHE245 |
| B | THR246 |
| B | GLY247 |
| B | SER248 |
| B | ILE251 |
| B | GLU267 |
| B | LEU268 |
| B | GLY269 |
| B | CYS302 |
| B | GLU396 |
| B | PHE398 |
| B | TYR463 |
| B | HOH604 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | binding site for residue NAP C 501 |
| Chain | Residue |
| C | VAL167 |
| C | SER168 |
| C | PRO169 |
| C | TRP170 |
| C | ASN171 |
| C | LEU176 |
| C | LYS194 |
| C | ALA196 |
| C | SER197 |
| C | VAL226 |
| C | ARG228 |
| C | ALA231 |
| C | PHE245 |
| C | THR246 |
| C | GLY247 |
| C | SER248 |
| C | ILE251 |
| C | GLU267 |
| C | LEU268 |
| C | GLY269 |
| C | CYS302 |
| C | GLU396 |
| C | PHE398 |
| C | TYR463 |
| C | HOH614 |
| C | HOH625 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 501 |
| Chain | Residue |
| D | GLU132 |
| D | ARG135 |
| D | LYS477 |
| D | MET480 |
| D | ASP481 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| C | VAL264 |
| C | GLN472 |
| D | LYS263 |
| D | VAL264 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | binding site for residue NAP D 503 |
| Chain | Residue |
| D | ALA231 |
| D | PHE245 |
| D | THR246 |
| D | GLY247 |
| D | SER248 |
| D | ILE251 |
| D | GLU267 |
| D | LEU268 |
| D | GLY269 |
| D | CYS302 |
| D | GLU396 |
| D | PHE398 |
| D | TYR463 |
| D | VAL167 |
| D | SER168 |
| D | PRO169 |
| D | TRP170 |
| D | ASN171 |
| D | LEU176 |
| D | LYS194 |
| D | ALA196 |
| D | SER197 |
| D | VAL226 |
| D | ARG228 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGNAP |
| Chain | Residue | Details |
| A | MET266-PRO273 |
