5ADH
INTERDOMAIN MOTION IN LIVER ALCOHOL DEHYDROGENASE. STRUCTURAL AND ENERGETIC ANALYSIS OF THE HINGE BENDING MODE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 375 |
| Chain | Residue |
| A | CYS46 |
| A | HIS67 |
| A | CYS174 |
| A | HOH419 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 376 |
| Chain | Residue |
| A | CYS97 |
| A | CYS100 |
| A | CYS103 |
| A | CYS111 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE APR A 377 |
| Chain | Residue |
| A | GLY199 |
| A | LEU200 |
| A | GLY201 |
| A | GLY202 |
| A | ASP223 |
| A | ILE224 |
| A | LYS228 |
| A | VAL268 |
| A | ILE269 |
| A | ARG271 |
| A | VAL292 |
| A | GLY293 |
| A | HOH388 |
| A | HOH421 |
| A | HOH422 |
| A | HOH664 |
| A | HOH668 |
| A | HOH669 |
| A | HOH670 |
| A | ARG47 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 378 |
| Chain | Residue |
| A | SER48 |
| A | LEU116 |
| A | VAL294 |
| A | PRO296 |
| A | LEU309 |
| A | HOH657 |
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 | ARG47 | |
| A | GLU68 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06525 |
| Chain | Residue | Details |
| A | ASP49 | |
| A | GLY293 | |
| A | GLY320 |
| Chain | Residue | Details |
| A | GLY98 | |
| A | ARG101 | |
| A | LYS104 | |
| A | LEU112 |
| Chain | Residue | Details |
| A | GLY175 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| 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 | LEU200 |
| Chain | Residue | Details |
| A | ILE224 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| 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 | PHE229 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| 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 | THR370 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:5466062 |
| Chain | Residue | Details |
| A | THR2 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| A | LEU57 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| A | SER48 | |
| A | HIS51 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 256 |
| Chain | Residue | Details |
| A | ARG47 | metal ligand |
| A | ASP49 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | VAL52 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | GLU68 | metal ligand |
| A | GLY175 | metal ligand |
