6CZP
2.2 Angstrom Resolution Crystal Structure Oxygen-Insensitive NAD(P)H-dependent Nitroreductase NfsB from Vibrio vulnificus in Complex with FMN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0005829 | cellular_component | cytosol |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0005829 | cellular_component | cytosol |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
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 | ILE164 |
| A | GLU165 |
| A | GLY166 |
| A | LYS205 |
| A | ARG207 |
| A | HOH414 |
| A | HOH422 |
| A | HOH441 |
| B | ALA38 |
| B | SER39 |
| A | TYR11 |
| B | SER40 |
| B | ASN42 |
| B | GLN142 |
| B | LEU145 |
| B | HOH435 |
| A | SER12 |
| A | LYS14 |
| A | PHE70 |
| A | ASN71 |
| A | LYS74 |
| A | TYR144 |
| A | PRO163 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue FMN B 301 |
| Chain | Residue |
| A | ALA38 |
| A | SER39 |
| A | SER40 |
| A | ASN42 |
| A | GLN142 |
| A | LEU145 |
| A | HOH464 |
| B | ARG10 |
| B | TYR11 |
| B | SER12 |
| B | LYS14 |
| B | PHE70 |
| B | ASN71 |
| B | TYR144 |
| B | PRO163 |
| B | ILE164 |
| B | GLU165 |
| B | GLY166 |
| B | LYS205 |
| B | ARG207 |
| B | HOH444 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| A | PHE70 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 303 |
| Chain | Residue |
| A | THR215 |
| B | HIS47 |
| B | LEU178 |
| B | LYS181 |
| B | PHE183 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | binding site for residue FMN C 301 |
| Chain | Residue |
| C | ARG10 |
| C | TYR11 |
| C | SER12 |
| C | LYS14 |
| C | PHE70 |
| C | ASN71 |
| C | LYS74 |
| C | TYR144 |
| C | PRO163 |
| C | ILE164 |
| C | GLU165 |
| C | GLY166 |
| C | LYS205 |
| C | ARG207 |
| C | HOH452 |
| D | ALA38 |
| D | SER39 |
| D | SER40 |
| D | ASN42 |
| D | GLN142 |
| D | LEU145 |
| D | HOH426 |
| D | HOH453 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 302 |
| Chain | Residue |
| C | ASN115 |
| H | VAL111 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue PGE C 303 |
| Chain | Residue |
| C | HIS47 |
| C | LYS181 |
| C | HOH443 |
| D | THR215 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for residue FMN D 301 |
| Chain | Residue |
| D | ARG207 |
| C | ALA38 |
| C | SER39 |
| C | SER40 |
| C | ASN42 |
| C | GLN142 |
| C | LEU145 |
| C | HOH413 |
| D | ARG10 |
| D | TYR11 |
| D | SER12 |
| D | LYS14 |
| D | ASN71 |
| D | LYS74 |
| D | TYR144 |
| D | PRO163 |
| D | ILE164 |
| D | GLU165 |
| D | GLY166 |
| D | LYS205 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 302 |
| Chain | Residue |
| D | ALA89 |
| D | ILE90 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue PEG D 303 |
| Chain | Residue |
| C | THR215 |
| D | HIS47 |
| D | LEU178 |
| D | LYS181 |
| D | PHE183 |
| site_id | AD2 |
| Number of Residues | 24 |
| Details | binding site for residue FMN E 301 |
| Chain | Residue |
| E | ARG10 |
| E | TYR11 |
| E | SER12 |
| E | LYS14 |
| E | ASN71 |
| E | LYS74 |
| E | TYR144 |
| E | PRO163 |
| E | ILE164 |
| E | GLU165 |
| E | GLY166 |
| E | LYS205 |
| E | ARG207 |
| E | HOH424 |
| E | HOH430 |
| E | HOH433 |
| E | HOH466 |
| F | ALA38 |
| F | SER39 |
| F | SER40 |
| F | ASN42 |
| F | GLN142 |
| F | LEU145 |
| F | HOH452 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL E 302 |
| Chain | Residue |
| E | GLN8 |
| E | SER9 |
| E | ARG10 |
| E | TYR11 |
| E | ALA201 |
| E | LEU203 |
| site_id | AD4 |
| Number of Residues | 21 |
| Details | binding site for residue FMN F 301 |
| Chain | Residue |
| E | ALA38 |
| E | SER39 |
| E | SER40 |
| E | ASN42 |
| E | GLN142 |
| E | LEU145 |
| F | ARG10 |
| F | TYR11 |
| F | SER12 |
| F | LYS14 |
| F | PHE70 |
| F | ASN71 |
| F | TYR144 |
| F | PRO163 |
| F | ILE164 |
| F | GLU165 |
| F | GLY166 |
| F | LYS205 |
| F | ARG207 |
| F | HOH450 |
| F | HOH463 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue PEG F 302 |
| Chain | Residue |
| E | GLY67 |
| F | PHE123 |
| site_id | AD6 |
| Number of Residues | 22 |
| Details | binding site for residue FMN G 301 |
| Chain | Residue |
| G | ARG10 |
| G | TYR11 |
| G | SER12 |
| G | LYS14 |
| G | PHE70 |
| G | ASN71 |
| G | LYS74 |
| G | TYR144 |
| G | PRO163 |
| G | ILE164 |
| G | GLU165 |
| G | GLY166 |
| G | LYS205 |
| G | ARG207 |
| G | HOH431 |
| H | ALA38 |
| H | SER39 |
| H | SER40 |
| H | VAL41 |
| H | ASN42 |
| H | GLN142 |
| H | LEU145 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue CL G 302 |
| Chain | Residue |
| G | ASP91 |
| G | GLU92 |
| G | ARG129 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue PGE G 303 |
| Chain | Residue |
| G | PHE176 |
| G | LEU178 |
| G | LYS181 |
| site_id | AD9 |
| Number of Residues | 22 |
| Details | binding site for residue FMN H 301 |
| Chain | Residue |
| G | ALA38 |
| G | SER39 |
| G | SER40 |
| G | ASN42 |
| G | GLN142 |
| G | LEU145 |
| H | ARG10 |
| H | TYR11 |
| H | SER12 |
| H | LYS14 |
| H | ASN71 |
| H | LYS74 |
| H | TYR144 |
| H | PRO163 |
| H | ILE164 |
| H | GLU165 |
| H | GLY166 |
| H | LYS205 |
| H | ARG207 |
| H | HOH416 |
| H | HOH425 |
| H | HOH441 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL H 302 |
| Chain | Residue |
| G | LEU132 |
| H | GLU165 |
| H | PHE167 |
| H | ALA169 |
| H | HOH424 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue PGE H 303 |
| Chain | Residue |
| G | THR215 |
| H | PHE176 |
| H | LEU178 |
| H | LYS181 |
