3RJ9
Structure of alcohol dehydrogenase from Drosophila lebanonesis T114V mutant complexed with NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006066 | biological_process | alcohol metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006066 | biological_process | alcohol metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006066 | biological_process | alcohol metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006066 | biological_process | alcohol metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042802 | molecular_function | identical protein binding |
| E | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006066 | biological_process | alcohol metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0042802 | molecular_function | identical protein binding |
| F | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006066 | biological_process | alcohol metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 850 |
| Chain | Residue |
| A | ALA12 |
| A | ALA92 |
| A | GLY93 |
| A | ILE106 |
| A | ILE136 |
| A | CYS137 |
| A | SER138 |
| A | TYR151 |
| A | LYS155 |
| A | PRO181 |
| A | GLY182 |
| A | GLY15 |
| A | ILE183 |
| A | THR184 |
| A | THR186 |
| A | PRO187 |
| A | LEU188 |
| A | HOH288 |
| A | HOH289 |
| A | HOH292 |
| A | HOH334 |
| A | HOH599 |
| A | GLY16 |
| A | HOH741 |
| A | HOH1004 |
| A | ILE17 |
| A | ASP37 |
| A | TYR62 |
| A | ASP63 |
| A | VAL64 |
| A | GLY91 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD B 850 |
| Chain | Residue |
| B | ALA12 |
| B | GLY15 |
| B | GLY16 |
| B | ILE17 |
| B | ASP37 |
| B | ARG38 |
| B | TYR62 |
| B | ASP63 |
| B | VAL64 |
| B | GLY91 |
| B | ALA92 |
| B | GLY93 |
| B | ILE106 |
| B | ILE136 |
| B | CYS137 |
| B | SER138 |
| B | TYR151 |
| B | LYS155 |
| B | PRO181 |
| B | GLY182 |
| B | ILE183 |
| B | THR184 |
| B | THR186 |
| B | LEU188 |
| B | HOH261 |
| B | HOH265 |
| B | HOH268 |
| B | HOH305 |
| B | HOH529 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD C 850 |
| Chain | Residue |
| C | ALA12 |
| C | GLY15 |
| C | GLY16 |
| C | ILE17 |
| C | ASP37 |
| C | ARG38 |
| C | ASP63 |
| C | VAL64 |
| C | GLY91 |
| C | ALA92 |
| C | GLY93 |
| C | ILE106 |
| C | ILE136 |
| C | CYS137 |
| C | SER138 |
| C | TYR151 |
| C | LYS155 |
| C | PRO181 |
| C | GLY182 |
| C | ILE183 |
| C | THR184 |
| C | THR186 |
| C | PRO187 |
| C | LEU188 |
| C | HOH255 |
| C | HOH280 |
| C | HOH286 |
| C | HOH493 |
| C | HOH707 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD D 850 |
| Chain | Residue |
| D | ALA92 |
| D | GLY93 |
| D | ILE106 |
| D | ILE136 |
| D | CYS137 |
| D | SER138 |
| D | TYR151 |
| D | LYS155 |
| D | PRO181 |
| D | GLY182 |
| D | ILE183 |
| D | THR184 |
| D | THR186 |
| D | LEU188 |
| D | HOH259 |
| D | HOH329 |
| D | HOH334 |
| D | HOH367 |
| D | HOH513 |
| D | ALA12 |
| D | GLY15 |
| D | GLY16 |
| D | ILE17 |
| D | ASP37 |
| D | ARG38 |
| D | TYR62 |
| D | ASP63 |
| D | VAL64 |
| D | GLY91 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD E 850 |
| Chain | Residue |
| E | ALA12 |
| E | GLY15 |
| E | GLY16 |
| E | ILE17 |
| E | ASP37 |
| E | ARG38 |
| E | TYR62 |
| E | ASP63 |
| E | VAL64 |
| E | GLY91 |
| E | ALA92 |
| E | GLY93 |
| E | ILE106 |
| E | ILE136 |
| E | CYS137 |
| E | SER138 |
| E | TYR151 |
| E | LYS155 |
| E | PRO181 |
| E | GLY182 |
| E | ILE183 |
| E | THR184 |
| E | THR186 |
| E | LEU188 |
| E | HOH256 |
| E | HOH273 |
| E | HOH278 |
| E | HOH311 |
| E | HOH676 |
| E | HOH951 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD F 850 |
| Chain | Residue |
| F | ALA12 |
| F | GLY15 |
| F | GLY16 |
| F | ILE17 |
| F | ASP37 |
| F | TYR62 |
| F | ASP63 |
| F | VAL64 |
| F | GLY91 |
| F | ALA92 |
| F | GLY93 |
| F | ILE106 |
| F | ILE136 |
| F | CYS137 |
| F | SER138 |
| F | TYR151 |
| F | LYS155 |
| F | PRO181 |
| F | GLY182 |
| F | THR184 |
| F | THR186 |
| F | LEU188 |
| F | VAL189 |
| F | HOH266 |
| F | HOH604 |
| F | HOH1002 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvtgfnaihqVpvYSASKAAVvSFTnSLA |
| Chain | Residue | Details |
| A | SER138-ALA166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 138 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10366509","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"2707261","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
