6DXP
The crystal structure of an FMN-dependent NADH-azoreductase from Klebsiella pneumoniae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| B | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| C | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| D | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue FMN A 301 |
| Chain | Residue |
| A | SER10 |
| A | LEU98 |
| A | SER139 |
| A | ARG140 |
| A | GLY141 |
| A | GLY142 |
| A | GLN145 |
| A | GLU147 |
| A | LEU176 |
| A | HOH406 |
| B | LEU51 |
| A | ASN12 |
| B | PHE56 |
| A | SER16 |
| A | LEU17 |
| A | THR18 |
| A | PRO94 |
| A | MET95 |
| A | TYR96 |
| A | ASN97 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue FMN C 301 |
| Chain | Residue |
| C | SER10 |
| C | ASN12 |
| C | SER16 |
| C | LEU17 |
| C | THR18 |
| C | PRO94 |
| C | MET95 |
| C | TYR96 |
| C | ASN97 |
| C | LEU98 |
| C | SER139 |
| C | ARG140 |
| C | GLY141 |
| C | GLY142 |
| C | GLN145 |
| C | GLU147 |
| C | LEU176 |
| D | LEU51 |
| D | PHE56 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue FMN B 301 |
| Chain | Residue |
| A | LEU51 |
| A | PHE56 |
| B | SER10 |
| B | ASN12 |
| B | SER16 |
| B | LEU17 |
| B | THR18 |
| B | PRO94 |
| B | MET95 |
| B | TYR96 |
| B | ASN97 |
| B | LEU98 |
| B | SER139 |
| B | ARG140 |
| B | GLY141 |
| B | GLY142 |
| B | GLN145 |
| B | GLU147 |
| B | LEU176 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | binding site for residue FMN D 301 |
| Chain | Residue |
| C | LEU51 |
| C | PHE56 |
| D | SER10 |
| D | ASN12 |
| D | SER16 |
| D | LEU17 |
| D | THR18 |
| D | PRO94 |
| D | MET95 |
| D | TYR96 |
| D | ASN97 |
| D | LEU98 |
| D | SER139 |
| D | ARG140 |
| D | GLY141 |
| D | GLY142 |
| D | GLN145 |
| D | GLU147 |
| D | LEU176 |
