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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD A 255 |
| Chain | Residue |
| A | ALA12 |
| A | GLY15 |
| A | GLY16 |
| A | ILE17 |
| A | ASP37 |
| A | ARG38 |
| A | TYR62 |
| A | ASP63 |
| A | VAL64 |
| A | GLY91 |
| A | ALA92 |
| A | GLY93 |
| A | ILE106 |
| A | ILE136 |
| A | CYS137 |
| A | SER138 |
| A | TYR151 |
| A | LYS155 |
| A | PRO181 |
| A | GLY182 |
| A | THR184 |
| A | THR186 |
| A | LEU188 |
| A | VAL189 |
| A | HOH259 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD B 256 |
| 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 | THR184 |
| B | THR186 |
| B | LEU188 |
| B | VAL189 |
| site_id | ACA |
| Number of Residues | 3 |
| Details | CATALYTIC TRIAD |
| Chain | Residue |
| A | SER138 |
| A | TYR151 |
| A | LYS155 |
| site_id | ACB |
| Number of Residues | 3 |
| Details | CATALYTIC TRIAD |
| Chain | Residue |
| B | SER138 |
| B | TYR151 |
| B | LYS155 |
| site_id | CAA |
| Number of Residues | 2 |
| Details | CA2+ BINDING RESIDUES |
| site_id | CAB |
| Number of Residues | 2 |
| Details | CA2+ BINDING RESIDUES |
| site_id | NA1 |
| Number of Residues | 3 |
| Details | NAD BINDING MOTIF IN DADHS G(A)XGXXG |
| Chain | Residue |
| A | ALA13 |
| A | GLY15 |
| A | GLY18 |
| site_id | NA2 |
| Number of Residues | 3 |
| Details | NAD BINDING MOTIF IN SDRS GXXXGXG |
| Chain | Residue |
| A | ALA12 |
| A | GLY16 |
| A | GLY18 |
| site_id | NA3 |
| Number of Residues | 1 |
| Details | NAD/NADP SELECTIVITY AMINO ACID |
| site_id | NB1 |
| Number of Residues | 3 |
| Details | NAD BINDING MOTIF IN DADHS G(A)XGXXG |
| Chain | Residue |
| B | ALA13 |
| B | GLY15 |
| B | GLY18 |
| site_id | NB2 |
| Number of Residues | 3 |
| Details | NAD BINDING MOTIF IN SDRS GXXXGXG |
| Chain | Residue |
| B | ALA12 |
| B | GLY16 |
| B | GLY18 |
| site_id | NB3 |
| Number of Residues | 1 |
| Details | NAD/NADP SELECTIVITY AMINO ACID |
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 | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 46 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10366509","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"2707261","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS155 | |
| A | SER138 | |
| A | TYR151 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS155 | |
| B | SER138 | |
| B | TYR151 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS155 | |
| A | ASN107 | |
| A | SER138 | |
| A | TYR151 | |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS155 | |
| B | ASN107 | |
| B | SER138 | |
| B | TYR151 | |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS155 | |
| A | VAL148 | |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS155 | |
| B | VAL148 | |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS155 | |
| A | TYR151 | |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS155 | |
| B | TYR151 | |
