3OWO
Structures of iron-dependent alcohol dehydrogenase 2 from Zymomonas mobilis ZM4 with and without 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 | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 384 |
| Chain | Residue |
| A | ASP194 |
| A | HIS198 |
| A | HIS263 |
| A | HIS277 |
| A | ASN281 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 B 384 |
| Chain | Residue |
| B | HOH507 |
| B | HOH522 |
| B | ASP194 |
| B | HIS198 |
| B | HIS263 |
| B | HIS277 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 C 384 |
| Chain | Residue |
| C | ASP194 |
| C | HIS198 |
| C | HIS263 |
| C | HIS277 |
| C | ASN281 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 D 384 |
| Chain | Residue |
| D | ASP194 |
| D | HIS198 |
| D | HIS263 |
| D | HIS277 |
| D | HOH510 |
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 |
