5ILG
Crystal structure of photoreceptor dehydrogenase from Drosophila melanogaster
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0042574 | biological_process | retinal metabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0042572 | biological_process | retinol metabolic process |
| B | 0042574 | biological_process | retinal metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | GLY92 |
| A | ILE93 |
| A | NAD302 |
| A | HOH497 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | binding site for residue NAD A 302 |
| Chain | Residue |
| A | LEU38 |
| A | MET62 |
| A | ASP63 |
| A | VAL64 |
| A | VAL90 |
| A | ALA91 |
| A | GLY92 |
| A | ILE93 |
| A | ARG101 |
| A | VAL105 |
| A | MET135 |
| A | SER136 |
| A | TYR150 |
| A | LYS154 |
| A | PRO182 |
| A | GLY183 |
| A | ALA184 |
| A | THR185 |
| A | THR187 |
| A | PHE190 |
| A | MG301 |
| A | IPH303 |
| A | EDO306 |
| A | HOH419 |
| A | HOH421 |
| A | HOH431 |
| A | HOH432 |
| A | HOH470 |
| A | GLY12 |
| A | GLY15 |
| A | GLY16 |
| A | ILE17 |
| A | ASP37 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue IPH A 303 |
| Chain | Residue |
| A | SER137 |
| A | TYR150 |
| A | ALA184 |
| A | ILE209 |
| A | NAD302 |
| A | EDO304 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | GLY183 |
| A | ALA184 |
| A | ARG212 |
| A | IPH303 |
| A | HOH402 |
| A | HOH499 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | GLY5 |
| A | GLY29 |
| A | ALA31 |
| A | HOH468 |
| B | ASP188 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | ALA14 |
| A | ASP37 |
| A | GLN39 |
| A | NAD302 |
| A | HOH432 |
| A | HOH457 |
| A | HOH457 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | GLY16 |
| B | THR187 |
| B | ASP188 |
| B | NAD302 |
| site_id | AC8 |
| Number of Residues | 30 |
| Details | binding site for residue NAD B 302 |
| Chain | Residue |
| B | GLY12 |
| B | GLY15 |
| B | GLY16 |
| B | ILE17 |
| B | ASP37 |
| B | LEU38 |
| B | MET62 |
| B | ASP63 |
| B | VAL64 |
| B | VAL90 |
| B | ALA91 |
| B | GLY92 |
| B | ILE93 |
| B | VAL105 |
| B | MET135 |
| B | SER136 |
| B | TYR150 |
| B | LYS154 |
| B | PRO182 |
| B | GLY183 |
| B | THR185 |
| B | THR187 |
| B | MET189 |
| B | PHE190 |
| B | MG301 |
| B | IPH303 |
| B | HOH412 |
| B | HOH435 |
| B | HOH451 |
| B | HOH461 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue IPH B 303 |
| Chain | Residue |
| B | PHE190 |
| B | NAD302 |
| B | SER137 |
| B | TYR150 |
| B | PRO182 |
| B | ALA184 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvvgldpmfiIpvYGATKAGIiNFTrCLA |
| Chain | Residue | Details |
| A | SER137-ALA165 |
