5MNS
Structural and functional characterization of OleP in complex with 6DEB in sodium formate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| F | 0020037 | molecular_function | heme binding |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | VAL93 |
| A | ARG298 |
| A | PHE321 |
| A | ALA348 |
| A | PHE349 |
| A | GLY350 |
| A | HIS354 |
| A | CYS356 |
| A | DEB502 |
| A | HOH628 |
| A | HOH636 |
| A | LEU94 |
| A | HIS101 |
| A | ARG105 |
| A | PHE112 |
| A | ALA244 |
| A | GLY245 |
| A | THR248 |
| A | GLN252 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue DEB A 502 |
| Chain | Residue |
| A | PHE84 |
| A | LEU94 |
| A | THR248 |
| A | PHE296 |
| A | LEU396 |
| A | HEM501 |
| A | HOH628 |
| A | HOH645 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | VAL93 |
| B | LEU94 |
| B | HIS101 |
| B | ARG105 |
| B | ILE157 |
| B | ALA244 |
| B | GLY245 |
| B | THR248 |
| B | GLN252 |
| B | ARG298 |
| B | PHE321 |
| B | ALA348 |
| B | PHE349 |
| B | GLY350 |
| B | HIS354 |
| B | CYS356 |
| B | ILE357 |
| B | DEB502 |
| B | HOH614 |
| B | HOH636 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue DEB B 502 |
| Chain | Residue |
| B | LEU94 |
| B | ILE243 |
| B | THR248 |
| B | LEU396 |
| B | HEM501 |
| B | HOH614 |
| B | HOH615 |
| B | HOH641 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for residue HEM C 501 |
| Chain | Residue |
| C | VAL93 |
| C | LEU94 |
| C | HIS101 |
| C | PHE112 |
| C | ALA244 |
| C | GLY245 |
| C | THR248 |
| C | GLN252 |
| C | LEU290 |
| C | ARG298 |
| C | PHE321 |
| C | ALA348 |
| C | PHE349 |
| C | GLY350 |
| C | HIS354 |
| C | CYS356 |
| C | ILE357 |
| C | LEU366 |
| C | DEB502 |
| C | HOH614 |
| C | HOH652 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue DEB C 502 |
| Chain | Residue |
| C | PHE84 |
| C | LEU94 |
| C | LEU179 |
| C | ILE243 |
| C | ALA244 |
| C | THR248 |
| C | PHE296 |
| C | LEU396 |
| C | ILE397 |
| C | HEM501 |
| C | HOH614 |
| C | HOH620 |
| C | HOH671 |
| C | HOH694 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue HEM D 501 |
| Chain | Residue |
| D | ARG298 |
| D | PHE321 |
| D | ALA348 |
| D | PHE349 |
| D | GLY350 |
| D | HIS354 |
| D | CYS356 |
| D | ILE357 |
| D | DEB502 |
| D | HOH602 |
| D | VAL93 |
| D | LEU94 |
| D | HIS101 |
| D | ARG105 |
| D | PHE112 |
| D | ALA244 |
| D | GLY245 |
| D | THR248 |
| D | GLN252 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue DEB D 502 |
| Chain | Residue |
| D | PHE84 |
| D | LEU94 |
| D | LEU179 |
| D | ILE243 |
| D | ALA244 |
| D | THR248 |
| D | PHE296 |
| D | LEU396 |
| D | HEM501 |
| D | HOH602 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | binding site for residue HEM E 501 |
| Chain | Residue |
| E | VAL93 |
| E | LEU94 |
| E | HIS101 |
| E | ARG105 |
| E | ALA244 |
| E | GLY245 |
| E | THR248 |
| E | SER249 |
| E | LEU290 |
| E | ARG298 |
| E | PHE321 |
| E | ALA348 |
| E | PHE349 |
| E | GLY350 |
| E | HIS354 |
| E | CYS356 |
| E | ILE357 |
| E | GLY362 |
| E | DEB502 |
| E | HOH601 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue DEB E 502 |
| Chain | Residue |
| E | LEU94 |
| E | LEU179 |
| E | ILE243 |
| E | ALA244 |
| E | THR248 |
| E | SER295 |
| E | PHE296 |
| E | HEM501 |
| E | HOH601 |
| E | HOH616 |
| site_id | AD2 |
| Number of Residues | 21 |
| Details | binding site for residue HEM F 501 |
| Chain | Residue |
| F | VAL93 |
| F | LEU94 |
| F | HIS101 |
| F | ARG105 |
| F | PHE112 |
| F | ALA244 |
| F | GLY245 |
| F | THR248 |
| F | LEU290 |
| F | ARG298 |
| F | PHE321 |
| F | ALA348 |
| F | PHE349 |
| F | GLY350 |
| F | HIS354 |
| F | CYS356 |
| F | ILE357 |
| F | GLY358 |
| F | DEB502 |
| F | HOH604 |
| F | HOH610 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue DEB F 502 |
| Chain | Residue |
| F | MET83 |
| F | PHE84 |
| F | LEU94 |
| F | ILE243 |
| F | THR248 |
| F | PHE296 |
| F | HEM501 |
| F | HOH604 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGAHHCIG |
| Chain | Residue | Details |
| A | PHE349-GLY358 |
