1KQD
Structure of Nitroreductase from E. cloacae Bound with 2e-Reduced Flavin Mononucleotide (FMN)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| A | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| B | 0005829 | cellular_component | cytosol |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| B | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| C | 0005829 | cellular_component | cytosol |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| C | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| D | 0005829 | cellular_component | cytosol |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| D | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN A 518 |
| Chain | Residue |
| A | ARG10 |
| A | GLU165 |
| A | GLY166 |
| A | LYS205 |
| A | ARG207 |
| A | HOH547 |
| A | HOH565 |
| A | HOH571 |
| A | HOH576 |
| B | PRO38 |
| B | SER39 |
| A | HIS11 |
| B | SER40 |
| B | THR41 |
| B | ASN42 |
| B | GLN142 |
| B | LEU145 |
| B | HOH632 |
| A | SER12 |
| A | LYS14 |
| A | ASN71 |
| A | LYS74 |
| A | TYR144 |
| A | PRO163 |
| A | ILE164 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN B 519 |
| Chain | Residue |
| A | PRO38 |
| A | SER39 |
| A | SER40 |
| A | ASN42 |
| A | GLN142 |
| A | LEU145 |
| A | HOH605 |
| B | ARG10 |
| B | HIS11 |
| B | SER12 |
| B | LYS14 |
| B | ASN71 |
| B | LYS74 |
| B | TYR144 |
| B | PRO163 |
| B | ILE164 |
| B | GLU165 |
| B | GLY166 |
| B | LYS205 |
| B | ARG207 |
| B | HOH527 |
| B | HOH552 |
| B | HOH555 |
| B | HOH556 |
| B | HOH631 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN C 520 |
| Chain | Residue |
| C | ARG10 |
| C | HIS11 |
| C | SER12 |
| C | LYS14 |
| C | ASN71 |
| C | LYS74 |
| C | TYR144 |
| C | PRO163 |
| C | ILE164 |
| C | GLU165 |
| C | GLY166 |
| C | LYS205 |
| C | ARG207 |
| C | HOH541 |
| C | HOH556 |
| C | HOH561 |
| C | HOH564 |
| D | PRO38 |
| D | SER39 |
| D | SER40 |
| D | ASN42 |
| D | GLN142 |
| D | LEU145 |
| D | HOH643 |
| D | HOH644 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN D 521 |
| Chain | Residue |
| D | HOH645 |
| C | PRO38 |
| C | SER39 |
| C | SER40 |
| C | ASN42 |
| C | GLN142 |
| C | LEU145 |
| D | ARG10 |
| D | HIS11 |
| D | SER12 |
| D | LYS14 |
| D | ASN71 |
| D | LYS74 |
| D | TYR144 |
| D | PRO163 |
| D | ILE164 |
| D | GLU165 |
| D | GLY166 |
| D | ASN200 |
| D | LYS205 |
| D | ARG207 |
| D | HOH537 |
| D | HOH538 |
| D | HOH541 |
| D | HOH572 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28578873, ECO:0007744|PDB:5J8D |
| Chain | Residue | Details |
| A | ARG10 | |
| D | ARG10 | |
| D | GLU165 | |
| D | LYS205 | |
| A | GLU165 | |
| A | LYS205 | |
| B | ARG10 | |
| B | GLU165 | |
| B | LYS205 | |
| C | ARG10 | |
| C | GLU165 | |
| C | LYS205 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:28578873, ECO:0007744|PDB:5J8D |
| Chain | Residue | Details |
| A | LYS14 | |
| B | ASN71 | |
| B | LYS74 | |
| B | ARG107 | |
| C | LYS14 | |
| C | THR41 | |
| C | THR67 | |
| C | ASN71 | |
| C | LYS74 | |
| C | ARG107 | |
| D | LYS14 | |
| A | THR41 | |
| D | THR41 | |
| D | THR67 | |
| D | ASN71 | |
| D | LYS74 | |
| D | ARG107 | |
| A | THR67 | |
| A | ASN71 | |
| A | LYS74 | |
| A | ARG107 | |
| B | LYS14 | |
| B | THR41 | |
| B | THR67 |
