3X21
Crystal structure of Escherichia coli nitroreductase NfsB mutant T41L/N71S/F124W
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 |
| E | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| E | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0010181 | molecular_function | FMN binding |
| E | 0016020 | cellular_component | membrane |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0042803 | molecular_function | protein homodimerization activity |
| E | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| E | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| F | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| F | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| F | 0005829 | cellular_component | cytosol |
| F | 0010181 | molecular_function | FMN binding |
| F | 0016020 | cellular_component | membrane |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0042803 | molecular_function | protein homodimerization activity |
| F | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| F | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| G | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| G | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| G | 0005829 | cellular_component | cytosol |
| G | 0010181 | molecular_function | FMN binding |
| G | 0016020 | cellular_component | membrane |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0042803 | molecular_function | protein homodimerization activity |
| G | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| G | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| H | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| H | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| H | 0005829 | cellular_component | cytosol |
| H | 0010181 | molecular_function | FMN binding |
| H | 0016020 | cellular_component | membrane |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0042802 | molecular_function | identical protein binding |
| H | 0042803 | molecular_function | protein homodimerization activity |
| H | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| H | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| I | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| I | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| I | 0005829 | cellular_component | cytosol |
| I | 0010181 | molecular_function | FMN binding |
| I | 0016020 | cellular_component | membrane |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0042802 | molecular_function | identical protein binding |
| I | 0042803 | molecular_function | protein homodimerization activity |
| I | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| I | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| J | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| J | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| J | 0005829 | cellular_component | cytosol |
| J | 0010181 | molecular_function | FMN binding |
| J | 0016020 | cellular_component | membrane |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0042802 | molecular_function | identical protein binding |
| J | 0042803 | molecular_function | protein homodimerization activity |
| J | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| J | 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 | 17 |
| Details | BINDING SITE FOR RESIDUE FMN A 301 |
| Chain | Residue |
| A | ARG10 |
| A | GLY166 |
| A | LYS205 |
| A | ARG207 |
| B | PRO38 |
| B | SER39 |
| B | SER40 |
| B | GLN142 |
| B | LEU145 |
| A | HIS11 |
| A | SER12 |
| A | LYS14 |
| A | LYS74 |
| A | TYR144 |
| A | PRO163 |
| A | ILE164 |
| A | GLU165 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN B 301 |
| Chain | Residue |
| A | PRO38 |
| A | SER39 |
| A | SER40 |
| A | ASN42 |
| A | GLN142 |
| A | LEU145 |
| B | ARG10 |
| B | HIS11 |
| B | SER12 |
| B | LYS14 |
| B | LYS74 |
| B | TYR144 |
| B | PRO163 |
| B | ILE164 |
| B | GLU165 |
| B | GLY166 |
| B | LYS205 |
| B | ARG207 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FMN C 301 |
| Chain | Residue |
| C | ARG10 |
| C | HIS11 |
| C | SER12 |
| C | LYS14 |
| C | LYS74 |
| C | PRO163 |
| C | ILE164 |
| C | GLU165 |
| C | GLY166 |
| C | LYS205 |
| C | ARG207 |
| D | PRO38 |
| D | SER39 |
| D | SER40 |
| D | ASN42 |
| D | LEU145 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN D 301 |
| Chain | Residue |
| C | PRO38 |
| C | SER39 |
| C | SER40 |
| C | GLN142 |
| C | LEU145 |
| D | ARG10 |
| D | HIS11 |
| D | SER12 |
| D | LYS14 |
| D | LYS74 |
| D | TYR144 |
| D | PRO163 |
| D | ILE164 |
| D | GLU165 |
| D | GLY166 |
| D | LYS205 |
| D | ARG207 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN E 301 |
| Chain | Residue |
| E | ARG10 |
| E | HIS11 |
| E | SER12 |
| E | LYS14 |
| E | LYS74 |
| E | PRO163 |
| E | ILE164 |
| E | GLU165 |
| E | GLY166 |
| E | ASN200 |
| E | LYS205 |
| E | ARG207 |
| F | PRO38 |
| F | SER39 |
| F | SER40 |
| F | ASN42 |
| F | GLN142 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN F 301 |
| Chain | Residue |
| F | GLY166 |
| F | LYS205 |
| F | ARG207 |
| E | PRO38 |
| E | SER39 |
| E | SER40 |
| E | ASN42 |
| E | GLN142 |
| E | LEU145 |
| F | ARG10 |
| F | HIS11 |
| F | SER12 |
| F | LYS14 |
| F | LYS74 |
| F | PRO163 |
| F | ILE164 |
| F | GLU165 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN G 301 |
| Chain | Residue |
| G | ARG10 |
| G | HIS11 |
| G | SER12 |
| G | LYS14 |
| G | LYS74 |
| G | PRO163 |
| G | ILE164 |
| G | GLU165 |
| G | GLY166 |
| G | LYS205 |
| G | ARG207 |
| H | PRO38 |
| H | SER39 |
| H | SER40 |
| H | ASN42 |
| H | GLN142 |
| H | LEU145 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN H 301 |
| Chain | Residue |
| G | PRO38 |
| G | SER39 |
| G | SER40 |
| G | ASN42 |
| G | GLN142 |
| G | LEU145 |
| H | ARG10 |
| H | HIS11 |
| H | SER12 |
| H | LYS14 |
| H | LYS74 |
| H | PRO163 |
| H | ILE164 |
| H | GLU165 |
| H | GLY166 |
| H | ASN200 |
| H | LYS205 |
| H | ARG207 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FMN I 301 |
| Chain | Residue |
| I | ARG10 |
| I | HIS11 |
| I | SER12 |
| I | LYS14 |
| I | LYS74 |
| I | PRO163 |
| I | ILE164 |
| I | GLU165 |
| I | GLY166 |
| I | LYS205 |
| I | ARG207 |
| J | PRO38 |
| J | SER39 |
| J | SER40 |
| J | ASN42 |
| J | GLN142 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN J 301 |
| Chain | Residue |
| I | PRO38 |
| I | SER39 |
| I | SER40 |
| I | ASN42 |
| I | GLN142 |
| I | LEU145 |
| J | ARG10 |
| J | HIS11 |
| J | SER12 |
| J | LYS14 |
| J | PRO163 |
| J | ILE164 |
| J | GLU165 |
| J | GLY166 |
| J | ASN200 |
| J | LYS205 |
| J | ARG207 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| 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 | |
| E | ARG10 | |
| E | GLU165 | |
| E | LYS205 | |
| F | ARG10 | |
| F | GLU165 | |
| F | LYS205 | |
| G | ARG10 | |
| A | GLU165 | |
| G | GLU165 | |
| G | LYS205 | |
| H | ARG10 | |
| H | GLU165 | |
| H | LYS205 | |
| I | ARG10 | |
| I | GLU165 | |
| I | LYS205 | |
| J | ARG10 | |
| J | GLU165 | |
| A | LYS205 | |
| J | LYS205 | |
| B | ARG10 | |
| B | GLU165 | |
| B | LYS205 | |
| C | ARG10 | |
| C | GLU165 | |
| C | LYS205 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 50 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q01234 |
| Chain | Residue | Details |
| A | LYS14 | |
| B | ARG107 | |
| C | LYS14 | |
| C | LEU41 | |
| C | SER71 | |
| C | LYS74 | |
| C | ARG107 | |
| D | LYS14 | |
| D | LEU41 | |
| D | SER71 | |
| D | LYS74 | |
| A | LEU41 | |
| D | ARG107 | |
| E | LYS14 | |
| E | LEU41 | |
| E | SER71 | |
| E | LYS74 | |
| E | ARG107 | |
| F | LYS14 | |
| F | LEU41 | |
| F | SER71 | |
| F | LYS74 | |
| A | SER71 | |
| F | ARG107 | |
| G | LYS14 | |
| G | LEU41 | |
| G | SER71 | |
| G | LYS74 | |
| G | ARG107 | |
| H | LYS14 | |
| H | LEU41 | |
| H | SER71 | |
| H | LYS74 | |
| A | LYS74 | |
| H | ARG107 | |
| I | LYS14 | |
| I | LEU41 | |
| I | SER71 | |
| I | LYS74 | |
| I | ARG107 | |
| J | LYS14 | |
| J | LEU41 | |
| J | SER71 | |
| J | LYS74 | |
| A | ARG107 | |
| J | ARG107 | |
| B | LYS14 | |
| B | LEU41 | |
| B | SER71 | |
| 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 | MCSA10 |
| Number of Residues | 3 |
| Details | M-CSA 211 |
| Chain | Residue | Details |
| J | LYS14 | electrostatic stabiliser, hydrogen bond donor |
| J | LYS74 | electrostatic stabiliser, hydrogen bond donor |
| J | 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 |
| site_id | MCSA5 |
| Number of Residues | 3 |
| Details | M-CSA 211 |
| Chain | Residue | Details |
| E | LYS14 | electrostatic stabiliser, hydrogen bond donor |
| E | LYS74 | electrostatic stabiliser, hydrogen bond donor |
| E | GLU165 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA6 |
| Number of Residues | 3 |
| Details | M-CSA 211 |
| Chain | Residue | Details |
| F | LYS14 | electrostatic stabiliser, hydrogen bond donor |
| F | LYS74 | electrostatic stabiliser, hydrogen bond donor |
| F | GLU165 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA7 |
| Number of Residues | 3 |
| Details | M-CSA 211 |
| Chain | Residue | Details |
| G | LYS14 | electrostatic stabiliser, hydrogen bond donor |
| G | LYS74 | electrostatic stabiliser, hydrogen bond donor |
| G | GLU165 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA8 |
| Number of Residues | 3 |
| Details | M-CSA 211 |
| Chain | Residue | Details |
| H | LYS14 | electrostatic stabiliser, hydrogen bond donor |
| H | LYS74 | electrostatic stabiliser, hydrogen bond donor |
| H | GLU165 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA9 |
| Number of Residues | 3 |
| Details | M-CSA 211 |
| Chain | Residue | Details |
| I | LYS14 | electrostatic stabiliser, hydrogen bond donor |
| I | LYS74 | electrostatic stabiliser, hydrogen bond donor |
| I | GLU165 | electrostatic stabiliser, hydrogen bond donor |
