7N2X
The crystal structure of an FMN-dependent NADH:quinone oxidoreductase, AzoR from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050446 | molecular_function | azobenzene reductase (NADP+) activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01216","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16684776","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18337254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1V4B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D5I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Z98","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Z9B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Z9C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Z9D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
