6WT2
Crystal Structure of Putative NAD(P)H-Flavin Oxidoreductase from Neisseria meningitidis
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 |
| A | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| 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 |
| B | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| 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 |
| C | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| 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 |
| 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 | 5 |
| Details | binding site for residue NIO A 301 |
| Chain | Residue |
| A | VAL47 |
| A | ARG106 |
| B | TRP71 |
| B | GLY169 |
| B | FMN304 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ARG20 |
| A | HIS21 |
| A | HOH461 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue FMN A 303 |
| Chain | Residue |
| A | LYS17 |
| A | SER18 |
| A | ARG20 |
| A | GLY72 |
| A | TYR147 |
| A | CYS165 |
| A | PRO166 |
| A | VAL167 |
| A | GLU168 |
| A | GLY169 |
| A | LYS209 |
| A | ARG211 |
| A | HOH406 |
| A | HOH430 |
| A | HOH455 |
| A | HOH462 |
| A | HOH485 |
| B | PRO44 |
| B | SER45 |
| B | SER46 |
| B | ARG106 |
| B | GLN145 |
| B | ILE148 |
| B | NIO301 |
| A | ARG16 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue NIO B 301 |
| Chain | Residue |
| A | GLY169 |
| A | FMN303 |
| B | SER46 |
| B | VAL47 |
| B | ARG106 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| A | LEU42 |
| B | ARG16 |
| B | LYS209 |
| B | ARG211 |
| B | FMN304 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 303 |
| Chain | Residue |
| B | ARG20 |
| B | HIS21 |
| B | HOH455 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | binding site for residue FMN B 304 |
| Chain | Residue |
| A | PRO44 |
| A | SER45 |
| A | SER46 |
| A | ARG106 |
| A | GLN145 |
| A | ILE148 |
| A | NIO301 |
| B | ARG16 |
| B | SER18 |
| B | ARG20 |
| B | GLY72 |
| B | TYR147 |
| B | CYS165 |
| B | PRO166 |
| B | VAL167 |
| B | GLU168 |
| B | GLY169 |
| B | LYS209 |
| B | ARG211 |
| B | EDO302 |
| B | HOH433 |
| B | HOH470 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue NIO C 301 |
| Chain | Residue |
| C | SER46 |
| C | VAL47 |
| C | ARG106 |
| D | GLY169 |
| D | FMN304 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| C | ARG16 |
| C | THR208 |
| C | LYS209 |
| C | ARG211 |
| C | FMN304 |
| D | LEU42 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 303 |
| Chain | Residue |
| C | ARG20 |
| C | HIS21 |
| C | HOH472 |
| site_id | AD2 |
| Number of Residues | 25 |
| Details | binding site for residue FMN C 304 |
| Chain | Residue |
| D | PRO44 |
| D | SER45 |
| D | SER46 |
| D | GLY48 |
| D | ARG106 |
| D | GLN145 |
| D | ILE148 |
| D | NIO302 |
| C | ARG16 |
| C | LYS17 |
| C | SER18 |
| C | ARG20 |
| C | GLY72 |
| C | TYR147 |
| C | CYS165 |
| C | PRO166 |
| C | VAL167 |
| C | GLU168 |
| C | GLY169 |
| C | LYS209 |
| C | ARG211 |
| C | EDO302 |
| C | HOH421 |
| C | HOH454 |
| C | HOH488 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue FMT D 301 |
| Chain | Residue |
| A | PRO60 |
| A | GLN64 |
| C | ARG105 |
| D | PRO213 |
| D | GLU216 |
| D | HOH442 |
| D | HOH475 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue NIO D 302 |
| Chain | Residue |
| C | TRP71 |
| C | GLY169 |
| C | FMN304 |
| D | SER46 |
| D | VAL47 |
| D | ARG106 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 303 |
| Chain | Residue |
| D | ARG20 |
| D | HIS21 |
| D | HOH420 |
| site_id | AD6 |
| Number of Residues | 25 |
| Details | binding site for residue FMN D 304 |
| Chain | Residue |
| C | PRO44 |
| C | SER45 |
| C | SER46 |
| C | GLY48 |
| C | ARG106 |
| C | GLN145 |
| C | ILE148 |
| C | NIO301 |
| D | ARG16 |
| D | LYS17 |
| D | SER18 |
| D | ARG20 |
| D | GLY72 |
| D | TYR147 |
| D | CYS165 |
| D | PRO166 |
| D | VAL167 |
| D | GLU168 |
| D | GLY169 |
| D | LYS209 |
| D | ARG211 |
| D | HOH408 |
| D | HOH409 |
| D | HOH422 |
| D | HOH463 |
