Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050009 | molecular_function | isopropanol dehydrogenase (NADP+) activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050009 | molecular_function | isopropanol dehydrogenase (NADP+) activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050009 | molecular_function | isopropanol dehydrogenase (NADP+) activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050009 | molecular_function | isopropanol dehydrogenase (NADP+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 354 |
| Chain | Residue |
| A | CYS37 |
| A | SER39 |
| A | HIS59 |
| A | ASP150 |
| A | NAP353 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1354 |
| Chain | Residue |
| B | NAP1353 |
| B | CYS37 |
| B | SER39 |
| B | HIS59 |
| B | ASP150 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 2354 |
| Chain | Residue |
| C | CYS37 |
| C | SER39 |
| C | HIS59 |
| C | ASP150 |
| C | NAP2353 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 3354 |
| Chain | Residue |
| D | CYS37 |
| D | SER39 |
| D | ASP150 |
| D | NAP3353 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP A 353 |
| Chain | Residue |
| A | THR38 |
| A | SER39 |
| A | TRP110 |
| A | ASP150 |
| A | THR154 |
| A | GLY174 |
| A | ILE175 |
| A | GLY176 |
| A | PRO177 |
| A | VAL178 |
| A | VAL197 |
| A | GLY198 |
| A | SER199 |
| A | ARG200 |
| A | TYR218 |
| A | ALA242 |
| A | VAL265 |
| A | ASN266 |
| A | TYR267 |
| A | LYS340 |
| A | ZN354 |
| B | MET285 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAP B 1353 |
| Chain | Residue |
| A | MET285 |
| B | THR38 |
| B | SER39 |
| B | TRP110 |
| B | ASP150 |
| B | THR154 |
| B | GLY174 |
| B | ILE175 |
| B | GLY176 |
| B | PRO177 |
| B | VAL178 |
| B | VAL197 |
| B | GLY198 |
| B | SER199 |
| B | ARG200 |
| B | TYR218 |
| B | ALA242 |
| B | GLY244 |
| B | ASN245 |
| B | ASN266 |
| B | TYR267 |
| B | LYS340 |
| B | ZN1354 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP C 2353 |
| Chain | Residue |
| C | THR38 |
| C | SER39 |
| C | HIS42 |
| C | TRP110 |
| C | ASP150 |
| C | THR154 |
| C | GLY174 |
| C | ILE175 |
| C | GLY176 |
| C | PRO177 |
| C | VAL178 |
| C | VAL197 |
| C | SER199 |
| C | ARG200 |
| C | TYR218 |
| C | TYR267 |
| C | LYS340 |
| C | ZN2354 |
| D | MET285 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAP D 3353 |
| Chain | Residue |
| D | TYR267 |
| D | ZN3354 |
| C | MET285 |
| D | THR38 |
| D | SER39 |
| D | ASP150 |
| D | THR154 |
| D | GLY174 |
| D | ILE175 |
| D | GLY176 |
| D | PRO177 |
| D | VAL178 |
| D | SER199 |
| D | ARG200 |
| D | TYR218 |
| D | GLY244 |
| D | VAL265 |
| D | ASN266 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaVGEvvevGseV |
| Chain | Residue | Details |
| A | GLY58-VAL72 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | CYS37 | |
| D | CYS37 | |
| D | HIS59 | |
| D | ASP150 | |
| A | HIS59 | |
| A | ASP150 | |
| B | CYS37 | |
| B | HIS59 | |
| B | ASP150 | |
| C | CYS37 | |
| C | HIS59 | |
| C | ASP150 | |
| Chain | Residue | Details |
| A | ILE175 | |
| B | LYS340 | |
| C | ILE175 | |
| C | GLY198 | |
| C | TYR218 | |
| C | VAL265 | |
| C | LYS340 | |
| D | ILE175 | |
| D | GLY198 | |
| D | TYR218 | |
| D | VAL265 | |
| A | GLY198 | |
| D | LYS340 | |
| A | TYR218 | |
| A | VAL265 | |
| A | LYS340 | |
| B | ILE175 | |
| B | GLY198 | |
| B | TYR218 | |
| B | VAL265 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qlh |
| Chain | Residue | Details |
| A | HIS42 | |
| A | SER39 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qlh |
| Chain | Residue | Details |
| B | HIS42 | |
| B | SER39 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qlh |
| Chain | Residue | Details |
| C | HIS42 | |
| C | SER39 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qlh |
| Chain | Residue | Details |
| D | HIS42 | |
| D | SER39 | |
