1MG5
Crystal structure of Drosophila melanogaster alcohol dehydrogenase complexed with NADH and acetate at 1.6 A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006066 | biological_process | alcohol metabolic process |
| A | 0006067 | biological_process | ethanol metabolic process |
| A | 0006117 | biological_process | acetaldehyde metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019431 | biological_process | acetyl-CoA biosynthetic process from ethanol |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046164 | biological_process | alcohol catabolic process |
| A | 0048149 | biological_process | behavioral response to ethanol |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006066 | biological_process | alcohol metabolic process |
| B | 0006067 | biological_process | ethanol metabolic process |
| B | 0006117 | biological_process | acetaldehyde metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019431 | biological_process | acetyl-CoA biosynthetic process from ethanol |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046164 | biological_process | alcohol catabolic process |
| B | 0048149 | biological_process | behavioral response to ethanol |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 900 |
| Chain | Residue |
| A | SER139 |
| A | THR141 |
| A | TYR152 |
| A | ILE184 |
| A | NAI850 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 901 |
| Chain | Residue |
| B | NAI851 |
| B | SER139 |
| B | THR141 |
| B | TYR152 |
| B | ILE184 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAI A 850 |
| Chain | Residue |
| A | ALA13 |
| A | GLY16 |
| A | GLY17 |
| A | ILE18 |
| A | ASP38 |
| A | ARG39 |
| A | ILE40 |
| A | TYR63 |
| A | ASP64 |
| A | VAL65 |
| A | GLY92 |
| A | ALA93 |
| A | GLY94 |
| A | ARG103 |
| A | ILE137 |
| A | GLY138 |
| A | SER139 |
| A | TYR152 |
| A | LYS156 |
| A | PRO182 |
| A | GLY183 |
| A | ILE184 |
| A | THR185 |
| A | THR187 |
| A | LEU189 |
| A | ACT900 |
| A | HOH903 |
| A | HOH930 |
| A | HOH959 |
| A | HOH989 |
| A | HOH1028 |
| A | HOH1033 |
| A | HOH1067 |
| site_id | AC4 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAI B 851 |
| Chain | Residue |
| B | ALA13 |
| B | GLY16 |
| B | GLY17 |
| B | ILE18 |
| B | ASP38 |
| B | ARG39 |
| B | ILE40 |
| B | TYR63 |
| B | ASP64 |
| B | VAL65 |
| B | GLY92 |
| B | ALA93 |
| B | GLY94 |
| B | ARG103 |
| B | VAL107 |
| B | ILE137 |
| B | GLY138 |
| B | SER139 |
| B | TYR152 |
| B | LYS156 |
| B | PRO182 |
| B | GLY183 |
| B | ILE184 |
| B | THR185 |
| B | THR187 |
| B | LEU189 |
| B | ACT901 |
| B | HOH906 |
| B | HOH912 |
| B | HOH964 |
| B | HOH970 |
| B | HOH1009 |
| B | HOH1010 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvtgfnaiyqVpvYSGTKAAVvNFTsSLA |
| Chain | Residue | Details |
| A | SER139-ALA167 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15581900","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 64 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15581900","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"6821373","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | LYS156 | |
| A | SER139 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | LYS156 | |
| B | SER139 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | LYS156 | |
| A | SER139 | |
| A | ASN108 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | LYS156 | |
| B | SER139 | |
| B | ASN108 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS156 | |
| A | VAL149 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS156 | |
| B | VAL149 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | LYS156 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | LYS156 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 255 |
| Chain | Residue | Details |
| A | ASN108 | electrostatic stabiliser |
| A | SER139 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| A | TYR152 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS156 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 255 |
| Chain | Residue | Details |
| B | ASN108 | electrostatic stabiliser |
| B | SER139 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| B | TYR152 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | LYS156 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
