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 | 3 |
Details | ACTIVE SITE, CATALYIC TRIAD. |
Chain | Residue |
A | SER138 |
A | TYR151 |
A | LYS155 |
site_id | AC2 |
Number of Residues | 3 |
Details | ACTIVE SITE, CATALYIC TRIAD. |
Chain | Residue |
B | SER138 |
B | TYR151 |
B | LYS155 |
site_id | AC3 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAQ A 600 |
Chain | Residue |
A | ALA12 |
A | GLY15 |
A | GLY16 |
A | ILE17 |
A | ASP37 |
A | TYR62 |
A | ASP63 |
A | VAL64 |
A | GLY91 |
A | ALA92 |
A | GLY93 |
A | ILE106 |
A | ILE136 |
A | CYS137 |
A | SER138 |
A | VAL139 |
A | ILE145 |
A | TYR151 |
A | LYS155 |
A | PRO181 |
A | GLY182 |
A | ILE183 |
A | THR184 |
A | THR186 |
A | LEU188 |
A | HOH633 |
A | HOH641 |
A | HOH659 |
A | HOH724 |
A | HOH745 |
A | HOH850 |
site_id | AC4 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAQ B 500 |
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 | VAL139 |
B | ILE145 |
B | TYR151 |
B | LYS155 |
B | PRO181 |
B | GLY182 |
B | ILE183 |
B | THR184 |
B | THR186 |
B | LEU188 |
B | HOH538 |
B | HOH553 |
B | HOH649 |
B | HOH689 |
B | HOH696 |
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 AMINOACID |
site_id | NA4 |
Number of Residues | 3 |
Details | NAD BINDING MOTIF IN DADHS G(A)XGXXG |
Chain | Residue |
B | ALA13 |
B | GLY15 |
B | GLY18 |
site_id | NA5 |
Number of Residues | 3 |
Details | NAD BINDING MOTIF IN SDRS GXXXGXG |
Chain | Residue |
B | ALA12 |
B | GLY16 |
B | GLY18 |
site_id | NA6 |
Number of Residues | 1 |
Details | NAD/NADP SELECTIVITY AMINOACID |
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 | |