Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| A | 0008270 | molecular_function | zinc ion binding |
| 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | CYS93 |
| A | CYS96 |
| A | CYS99 |
| A | CYS107 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | CYS40 |
| A | HIS62 |
| A | CYS158 |
| A | HOH2375 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEiVGRvvavGdqV |
| Chain | Residue | Details |
| A | GLY61-VAL75 | |
| site_id | PS00065 |
| Number of Residues | 28 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGVVGiGGLGhmgiklahamgah.VVaFT |
| Chain | Residue | Details |
| A | VAL178-THR205 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS40 | |
| A | HIS62 | |
| A | CYS93 | |
| A | CYS96 | |
| A | CYS99 | |
| A | CYS107 | |
| A | CYS158 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| A | SER42 | |
| A | HIS41 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| A | TRP51 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| A | SER42 | |
| A | HIS45 | |
