6JXN
Crystal Structure of Indigo reductase from Bacillus smithii type strain DSM 4216
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor |
| B | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor |
| C | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H, NAD(P) 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 | 21 |
| Details | binding site for residue FMN A 301 |
| Chain | Residue |
| A | HIS10 |
| A | ALA146 |
| A | SER147 |
| A | GLY148 |
| A | GLY149 |
| A | TYR151 |
| A | GLN186 |
| A | ASN187 |
| A | HOH418 |
| A | HOH445 |
| A | HOH457 |
| A | SER17 |
| A | HOH463 |
| A | HOH487 |
| A | TYR18 |
| A | SER19 |
| A | PRO101 |
| A | MET102 |
| A | TRP103 |
| A | ASN104 |
| A | PHE105 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PE8 A 302 |
| Chain | Residue |
| A | GLU14 |
| A | THR15 |
| A | TYR18 |
| A | GLN194 |
| A | LYS197 |
| A | GLU198 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue FMN B 301 |
| Chain | Residue |
| B | HIS10 |
| B | SER17 |
| B | TYR18 |
| B | SER19 |
| B | PRO101 |
| B | MET102 |
| B | TRP103 |
| B | ASN104 |
| B | PHE105 |
| B | ALA146 |
| B | SER147 |
| B | GLY148 |
| B | GLY149 |
| B | TYR151 |
| B | GLN186 |
| B | ASN187 |
| B | HOH451 |
| B | HOH490 |
| B | HOH500 |
| C | ILE52 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue NHE B 302 |
| Chain | Residue |
| B | ALA119 |
| B | PHE125 |
| B | TYR127 |
| B | PHE172 |
| B | HOH401 |
| C | ASN104 |
| C | FMN301 |
| C | HOH496 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue NHE B 303 |
| Chain | Residue |
| B | SER106 |
| B | PHE107 |
| B | LYS112 |
| B | MET161 |
| B | TYR165 |
| C | SER106 |
| C | MET161 |
| C | TYR165 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | binding site for residue FMN C 301 |
| Chain | Residue |
| B | ILE52 |
| B | NHE302 |
| C | HIS10 |
| C | SER17 |
| C | TYR18 |
| C | SER19 |
| C | PRO101 |
| C | MET102 |
| C | TRP103 |
| C | ASN104 |
| C | PHE105 |
| C | ALA146 |
| C | SER147 |
| C | GLY148 |
| C | GLY149 |
| C | TYR151 |
| C | GLN186 |
| C | ASN187 |
| C | HOH407 |
| C | HOH426 |
| C | HOH444 |
| C | HOH467 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue PE8 C 302 |
| Chain | Residue |
| C | GLU14 |
| C | THR15 |
| C | SER17 |
| C | TYR18 |
| C | GLN194 |
| C | LYS197 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | binding site for residue FMN D 301 |
| Chain | Residue |
| D | TRP103 |
| D | ASN104 |
| D | PHE105 |
| D | ALA146 |
| D | SER147 |
| D | GLY148 |
| D | GLY149 |
| D | TYR151 |
| D | GLN186 |
| D | ASN187 |
| D | HOH428 |
| D | HOH431 |
| D | HOH458 |
| D | HOH474 |
| A | ILE52 |
| A | PHE57 |
| D | HIS10 |
| D | SER17 |
| D | TYR18 |
| D | SER19 |
| D | PRO101 |
| D | MET102 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue NHE D 302 |
| Chain | Residue |
| A | SER106 |
| A | PHE107 |
| A | LYS112 |
| A | MET161 |
| A | TYR165 |
| D | SER106 |
| D | PHE107 |
| D | LYS112 |
| D | MET161 |
| D | TYR165 |
