5J8D
Structure of nitroreductase from E. cloacae complexed with nicotinic acid adenine dinucleotide
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 | 24 |
| Details | binding site for residue FMN A 301 |
| Chain | Residue |
| A | ARG10 |
| A | GLY166 |
| A | ASN200 |
| A | LYS205 |
| A | ARG207 |
| A | DND302 |
| A | HOH457 |
| A | HOH473 |
| A | HOH491 |
| A | HOH537 |
| B | PRO38 |
| A | HIS11 |
| B | SER39 |
| B | SER40 |
| B | ASN42 |
| B | GLN142 |
| B | LEU145 |
| A | SER12 |
| A | LYS14 |
| A | ASN71 |
| A | LYS74 |
| A | PRO163 |
| A | ILE164 |
| A | GLU165 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue DND A 302 |
| Chain | Residue |
| A | LYS14 |
| A | THR67 |
| A | TYR68 |
| A | ASN71 |
| A | LYS74 |
| A | PHE199 |
| A | LEU203 |
| A | FMN301 |
| A | HOH404 |
| A | HOH429 |
| B | SER40 |
| B | THR41 |
| B | ARG107 |
| B | PHE124 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue DND A 303 |
| Chain | Residue |
| A | SER40 |
| A | THR41 |
| A | ARG107 |
| A | PHE108 |
| A | ALA113 |
| A | PHE124 |
| A | HOH407 |
| A | HOH408 |
| A | HOH449 |
| A | HOH475 |
| A | HOH492 |
| A | HOH513 |
| A | HOH523 |
| B | LYS14 |
| B | TYR68 |
| B | PHE70 |
| B | ASN71 |
| B | LYS74 |
| B | GLY166 |
| B | PHE199 |
| B | FMN301 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue FMN B 301 |
| Chain | Residue |
| A | PRO38 |
| A | SER39 |
| A | SER40 |
| A | ASN42 |
| A | LEU145 |
| A | DND303 |
| B | ARG10 |
| B | HIS11 |
| B | SER12 |
| B | LYS14 |
| B | ASN71 |
| B | LYS74 |
| B | VAL162 |
| B | PRO163 |
| B | ILE164 |
| B | GLU165 |
| B | GLY166 |
| B | LYS205 |
| B | ARG207 |
| B | HOH443 |
| B | HOH456 |
| B | HOH472 |
| B | HOH497 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | binding site for residue FMN C 301 |
| Chain | Residue |
| D | SER39 |
| D | SER40 |
| D | ASN42 |
| D | LEU145 |
| D | DND302 |
| C | ARG10 |
| C | HIS11 |
| C | SER12 |
| C | LYS14 |
| C | ASN71 |
| C | LYS74 |
| C | PRO163 |
| C | ILE164 |
| C | GLU165 |
| C | GLY166 |
| C | ASN200 |
| C | LYS205 |
| C | ARG207 |
| C | HOH403 |
| C | HOH427 |
| C | HOH447 |
| D | PRO38 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue DND C 302 |
| Chain | Residue |
| C | SER40 |
| C | THR41 |
| C | ARG107 |
| C | PHE108 |
| C | TYR123 |
| C | PHE124 |
| C | HOH404 |
| C | HOH411 |
| C | HOH488 |
| C | HOH574 |
| C | HOH576 |
| D | LYS14 |
| D | THR67 |
| D | TYR68 |
| D | ASN71 |
| D | LYS74 |
| D | GLY166 |
| D | PHE199 |
| D | FMN301 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | binding site for residue FMN D 301 |
| Chain | Residue |
| C | PRO38 |
| C | SER39 |
| C | SER40 |
| C | ASN42 |
| C | GLN142 |
| C | LEU145 |
| C | DND302 |
| D | ARG10 |
| D | HIS11 |
| D | SER12 |
| D | LYS14 |
| D | ASN71 |
| D | LYS74 |
| D | PRO163 |
| D | ILE164 |
| D | GLU165 |
| D | GLY166 |
| D | LYS205 |
| D | ARG207 |
| D | HOH440 |
| D | HOH472 |
| D | HOH507 |
| D | HOH520 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for residue DND D 302 |
| Chain | Residue |
| C | LYS14 |
| C | TYR68 |
| C | PHE70 |
| C | ASN71 |
| C | LYS74 |
| C | GLY166 |
| C | PHE199 |
| C | FMN301 |
| C | HOH492 |
| D | SER40 |
| D | THR41 |
| D | ARG107 |
| D | PHE108 |
| D | TYR123 |
| D | PHE124 |
| D | HOH422 |
| D | HOH515 |
| D | HOH566 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28578873","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5J8D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28578873","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5J8D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
