1YKI
The structure of E. coli nitroreductase bound with the antibiotic nitrofurazone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization 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 | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization 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 | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| C | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization 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 | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| D | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization 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 | 23 |
| Details | BINDING SITE FOR RESIDUE FMN A 1218 |
| Chain | Residue |
| A | ARG10 |
| A | GLY166 |
| A | LYS205 |
| A | ARG207 |
| A | NFZ1219 |
| A | HOH1229 |
| A | HOH1232 |
| A | HOH1233 |
| A | HOH1266 |
| B | PRO38 |
| B | SER39 |
| A | HIS11 |
| 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 | 10 |
| Details | BINDING SITE FOR RESIDUE NFZ A 1219 |
| Chain | Residue |
| A | ASN67 |
| A | TYR68 |
| A | PHE70 |
| A | ASN71 |
| A | GLU165 |
| A | FMN1218 |
| A | HOH1251 |
| A | HOH1421 |
| B | THR41 |
| B | PHE124 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN B 2218 |
| Chain | Residue |
| A | PRO38 |
| A | SER39 |
| A | SER40 |
| A | ASN42 |
| A | GLN142 |
| A | LEU145 |
| B | ARG10 |
| B | HIS11 |
| B | SER12 |
| B | LYS14 |
| B | ASN71 |
| B | LYS74 |
| B | PRO163 |
| B | ILE164 |
| B | GLU165 |
| B | GLY166 |
| B | ASN200 |
| B | LYS205 |
| B | ARG207 |
| B | NFZ2219 |
| B | HOH2229 |
| B | HOH2237 |
| B | HOH2239 |
| B | HOH2256 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NFZ B 2219 |
| Chain | Residue |
| A | THR41 |
| A | PHE124 |
| B | ASN67 |
| B | TYR68 |
| B | PHE70 |
| B | ASN71 |
| B | LYS74 |
| B | GLU165 |
| B | FMN2218 |
| B | HOH2290 |
| B | HOH2342 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN C 3218 |
| 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 | NFZ3219 |
| C | HOH4222 |
| C | HOH4233 |
| C | HOH4234 |
| C | HOH4241 |
| D | PRO38 |
| D | SER39 |
| D | SER40 |
| D | ASN42 |
| D | GLN142 |
| D | LEU145 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NFZ C 3219 |
| Chain | Residue |
| C | HOH4275 |
| C | HOH4289 |
| D | THR41 |
| D | PHE124 |
| C | ASN67 |
| C | TYR68 |
| C | PHE70 |
| C | ASN71 |
| C | GLU165 |
| C | FMN3218 |
| C | CIT4220 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN D 4218 |
| Chain | Residue |
| 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 | PRO163 |
| D | ILE164 |
| D | GLU165 |
| D | GLY166 |
| D | LYS205 |
| D | ARG207 |
| D | NFZ4219 |
| D | HOH4231 |
| D | HOH4236 |
| D | HOH4252 |
| D | HOH4261 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NFZ D 4219 |
| Chain | Residue |
| C | THR41 |
| C | PHE124 |
| D | ASN67 |
| D | TYR68 |
| D | PHE70 |
| D | ASN71 |
| D | GLU165 |
| D | FMN4218 |
| D | HOH4281 |
| D | HOH4301 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CIT C 4220 |
| Chain | Residue |
| C | LYS14 |
| C | LYS74 |
| C | PHE199 |
| C | NFZ3219 |
| C | HOH4275 |
| C | HOH4279 |
| C | HOH4307 |
| D | ASN117 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS C 1223 |
| Chain | Residue |
| C | LYS9 |
| C | ALA201 |
| C | LEU203 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS C 1224 |
| Chain | Residue |
| D | SER52 |
| D | HOH4274 |
| D | HOH4295 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS B 1225 |
| Chain | Residue |
| B | ALA104 |
| B | ASP105 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11020276, ECO:0000269|PubMed:11491290, ECO:0000269|PubMed:15684426 |
| 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 | 20 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q01234 |
| Chain | Residue | Details |
| A | LYS14 | |
| B | ARG107 | |
| C | LYS14 | |
| C | THR41 | |
| C | ASN71 | |
| C | LYS74 | |
| C | ARG107 | |
| D | LYS14 | |
| D | THR41 | |
| D | ASN71 | |
| D | LYS74 | |
| A | THR41 | |
| D | ARG107 | |
| A | ASN71 | |
| A | LYS74 | |
| A | ARG107 | |
| B | LYS14 | |
| B | THR41 | |
| B | ASN71 | |
| B | LYS74 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 211 |
| Chain | Residue | Details |
| A | LYS14 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS74 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU165 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 211 |
| Chain | Residue | Details |
| B | LYS14 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS74 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU165 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 211 |
| Chain | Residue | Details |
| C | LYS14 | electrostatic stabiliser, hydrogen bond donor |
| C | LYS74 | electrostatic stabiliser, hydrogen bond donor |
| C | GLU165 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 211 |
| Chain | Residue | Details |
| D | LYS14 | electrostatic stabiliser, hydrogen bond donor |
| D | LYS74 | electrostatic stabiliser, hydrogen bond donor |
| D | GLU165 | electrostatic stabiliser, hydrogen bond donor |
