7UTW
Cd-substituted Horse Liver Alcohol Dehydrogenase in Complex with NADH and N-Cyclohexylformamide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0042573 | biological_process | retinoic acid metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042572 | biological_process | retinol metabolic process |
| B | 0042573 | biological_process | retinoic acid metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaAGIvesiGegV |
| Chain | Residue | Details |
| A | GLY66-VAL80 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | CYS46 | |
| A | HIS67 | |
| B | CYS46 | |
| B | HIS67 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06525 |
| Chain | Residue | Details |
| A | SER48 | |
| A | VAL292 | |
| A | PHE319 | |
| B | SER48 | |
| B | VAL292 | |
| B | PHE319 |
| Chain | Residue | Details |
| A | CYS97 | |
| A | CYS100 | |
| A | CYS103 | |
| A | CYS111 | |
| B | CYS97 | |
| B | CYS100 | |
| B | CYS103 | |
| B | CYS111 |
| Chain | Residue | Details |
| A | CYS174 | |
| B | CYS174 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7, ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:6ADH |
| Chain | Residue | Details |
| A | GLY199 | |
| B | GLY199 |
| Chain | Residue | Details |
| A | ASP223 | |
| B | ASP223 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1QLH, ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH |
| Chain | Residue | Details |
| A | LYS228 | |
| B | LYS228 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7, ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:6ADH |
| Chain | Residue | Details |
| A | ARG369 | |
| B | ARG369 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:5466062 |
| Chain | Residue | Details |
| A | SER1 | |
| B | SER1 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 256 |
| Chain | Residue | Details |
| A | CYS46 | metal ligand |
| A | SER48 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS51 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS67 | metal ligand |
| A | CYS174 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 256 |
| Chain | Residue | Details |
| B | CYS46 | metal ligand |
| B | SER48 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | HIS51 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | HIS67 | metal ligand |
| B | CYS174 | metal ligand |
