3OX4
Structures of iron-dependent alcohol dehydrogenase 2 from Zymomonas mobilis ZM4 complexed with NAD cofactor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0120542 | molecular_function | ethanol dehydrogenase (NAD+) activity |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0120542 | molecular_function | ethanol dehydrogenase (NAD+) activity |
| C | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0120542 | molecular_function | ethanol dehydrogenase (NAD+) activity |
| D | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0120542 | molecular_function | ethanol dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD A 1385 |
| Chain | Residue |
| A | ASP39 |
| A | THR142 |
| A | PHE149 |
| A | ILE151 |
| A | LEU179 |
| A | GLY182 |
| A | MET183 |
| A | LEU187 |
| A | HIS277 |
| A | HOH431 |
| A | HOH457 |
| A | PHE41 |
| A | FE2501 |
| A | ASN71 |
| A | PRO72 |
| A | GLY97 |
| A | GLY98 |
| A | SER99 |
| A | THR138 |
| A | THR139 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 501 |
| Chain | Residue |
| A | ASP194 |
| A | HIS198 |
| A | HIS263 |
| A | HIS277 |
| A | NAD1385 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD B 1385 |
| Chain | Residue |
| B | ASP39 |
| B | PHE41 |
| B | MET42 |
| B | ASN71 |
| B | PRO72 |
| B | GLY97 |
| B | GLY98 |
| B | SER99 |
| B | PRO100 |
| B | ASP102 |
| B | THR138 |
| B | THR139 |
| B | THR142 |
| B | SER144 |
| B | THR147 |
| B | PHE149 |
| B | LEU179 |
| B | GLY182 |
| B | MET183 |
| B | PRO184 |
| B | LEU187 |
| B | PHE254 |
| B | HIS277 |
| B | HOH396 |
| B | HOH428 |
| B | HOH463 |
| B | HOH475 |
| B | FE2501 |
| B | HOH527 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 B 501 |
| Chain | Residue |
| B | ASP194 |
| B | HIS198 |
| B | HIS263 |
| B | HIS277 |
| B | NAD1385 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD C 1385 |
| Chain | Residue |
| C | ASP39 |
| C | PHE41 |
| C | MET42 |
| C | ASN71 |
| C | PRO72 |
| C | GLY97 |
| C | GLY98 |
| C | SER99 |
| C | ASP102 |
| C | THR138 |
| C | THR139 |
| C | THR142 |
| C | LEU179 |
| C | GLY182 |
| C | MET183 |
| C | PRO184 |
| C | LEU187 |
| C | ASP194 |
| C | HIS198 |
| C | HIS267 |
| C | HIS277 |
| C | HOH461 |
| C | FE2501 |
| C | HOH554 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 C 501 |
| Chain | Residue |
| C | ASP194 |
| C | HIS198 |
| C | HIS263 |
| C | HIS277 |
| C | ASN281 |
| C | NAD1385 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD D 1385 |
| Chain | Residue |
| D | LYS160 |
| D | LEU179 |
| D | GLY182 |
| D | MET183 |
| D | PRO184 |
| D | LEU187 |
| D | THR191 |
| D | HIS198 |
| D | HIS267 |
| D | HIS277 |
| D | HOH388 |
| D | HOH480 |
| D | FE2501 |
| D | ASP39 |
| D | PHE41 |
| D | ASN71 |
| D | GLY97 |
| D | GLY98 |
| D | SER99 |
| D | PRO100 |
| D | THR138 |
| D | THR139 |
| D | THR142 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 D 501 |
| Chain | Residue |
| D | ASP194 |
| D | HIS198 |
| D | HIS263 |
| D | HIS277 |
| D | NAD1385 |
Functional Information from PROSITE/UniProt
| site_id | PS00060 |
| Number of Residues | 21 |
| Details | ADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. GyVHamAHqLGGyynLpHGvC |
| Chain | Residue | Details |
| A | GLY260-CYS280 |
| site_id | PS00913 |
| Number of Residues | 29 |
| Details | ADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. SVnDpllmvgmPkgltAaTgmDALthafE |
| Chain | Residue | Details |
| A | SER173-GLU201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 56 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21295587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OX4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21295587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OWO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OX4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
