5MNV
Structural and functional characterization of OleP in complex with 6DEB in PEG
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
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 | 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 | 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 | 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 | 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 | 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 |
G | 0004497 | molecular_function | monooxygenase activity |
G | 0005506 | molecular_function | iron ion binding |
G | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
G | 0020037 | molecular_function | heme binding |
G | 0046872 | molecular_function | metal ion binding |
H | 0004497 | molecular_function | monooxygenase activity |
H | 0005506 | molecular_function | iron ion binding |
H | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
H | 0020037 | molecular_function | heme binding |
H | 0046872 | molecular_function | metal ion binding |
I | 0004497 | molecular_function | monooxygenase activity |
I | 0005506 | molecular_function | iron ion binding |
I | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
I | 0020037 | molecular_function | heme binding |
I | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | binding site for residue HEM A 501 |
Chain | Residue |
A | VAL93 |
A | GLN252 |
A | LEU290 |
A | PHE296 |
A | ARG298 |
A | ALA348 |
A | PHE349 |
A | GLY350 |
A | HIS354 |
A | CYS356 |
A | ILE357 |
A | LEU94 |
A | GLY358 |
A | DEB502 |
A | HOH605 |
A | HIS101 |
A | ARG105 |
A | LEU241 |
A | ALA244 |
A | GLY245 |
A | THR248 |
A | SER249 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue DEB A 502 |
Chain | Residue |
A | MET83 |
A | PHE84 |
A | ILE243 |
A | GLY294 |
A | LEU396 |
A | ILE397 |
A | HEM501 |
A | HOH605 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue HEM B 501 |
Chain | Residue |
B | VAL93 |
B | LEU94 |
B | HIS101 |
B | ARG105 |
B | ALA244 |
B | GLY245 |
B | THR248 |
B | ARG298 |
B | ALA348 |
B | PHE349 |
B | GLY350 |
B | HIS354 |
B | CYS356 |
B | DEB502 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue DEB B 502 |
Chain | Residue |
B | LEU94 |
B | SER240 |
B | ILE243 |
B | ALA244 |
B | THR248 |
B | SER295 |
B | PHE296 |
B | HEM501 |
site_id | AC5 |
Number of Residues | 18 |
Details | binding site for residue HEM C 501 |
Chain | Residue |
C | LEU94 |
C | HIS101 |
C | ARG105 |
C | PHE112 |
C | ALA244 |
C | GLY245 |
C | THR248 |
C | GLN252 |
C | ARG298 |
C | PHE321 |
C | ALA348 |
C | PHE349 |
C | GLY350 |
C | HIS354 |
C | CYS356 |
C | GLY358 |
C | LEU366 |
C | DEB502 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue DEB C 502 |
Chain | Residue |
C | PHE84 |
C | LEU94 |
C | SER240 |
C | ILE243 |
C | ALA244 |
C | SER295 |
C | PHE296 |
C | LEU396 |
C | HEM501 |
site_id | AC7 |
Number of Residues | 20 |
Details | binding site for residue HEM D 501 |
Chain | Residue |
D | VAL93 |
D | LEU94 |
D | HIS101 |
D | ARG105 |
D | LEU241 |
D | ALA244 |
D | GLY245 |
D | THR248 |
D | GLN252 |
D | LEU290 |
D | SER295 |
D | ARG298 |
D | PHE321 |
D | ALA348 |
D | PHE349 |
D | HIS354 |
D | CYS356 |
D | ILE357 |
D | GLY358 |
D | DEB502 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue DEB D 502 |
Chain | Residue |
D | MET83 |
D | LEU94 |
D | ILE243 |
D | ALA244 |
D | GLU247 |
D | THR248 |
D | GLY294 |
D | LEU396 |
D | HEM501 |
site_id | AC9 |
Number of Residues | 18 |
Details | binding site for residue HEM E 501 |
Chain | Residue |
E | VAL93 |
E | LEU94 |
E | HIS101 |
E | ARG105 |
E | LEU241 |
E | ALA244 |
E | GLY245 |
E | THR248 |
E | LEU290 |
E | PHE296 |
E | ARG298 |
E | PHE321 |
E | ALA348 |
E | PHE349 |
E | ALA353 |
E | HIS354 |
E | CYS356 |
E | DEB502 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue DEB E 502 |
Chain | Residue |
E | PHE84 |
E | LEU94 |
E | ALA244 |
E | GLU247 |
E | VAL291 |
E | SER295 |
E | LEU396 |
E | ILE397 |
E | HEM501 |
site_id | AD2 |
Number of Residues | 19 |
Details | binding site for residue HEM F 501 |
Chain | Residue |
F | VAL93 |
F | LEU94 |
F | HIS101 |
F | ARG105 |
F | LEU241 |
F | ALA244 |
F | GLY245 |
F | THR248 |
F | SER249 |
F | GLN252 |
F | ARG298 |
F | ALA348 |
F | PHE349 |
F | GLY350 |
F | HIS354 |
F | CYS356 |
F | GLY358 |
F | DEB502 |
F | HOH601 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue DEB F 502 |
Chain | Residue |
F | MET83 |
F | PHE84 |
F | ILE243 |
F | GLY294 |
F | LEU396 |
F | ILE397 |
F | HEM501 |
site_id | AD4 |
Number of Residues | 21 |
Details | binding site for residue HEM G 501 |
Chain | Residue |
G | VAL93 |
G | LEU94 |
G | HIS101 |
G | ARG105 |
G | LEU241 |
G | ALA244 |
G | GLY245 |
G | THR248 |
G | GLN252 |
G | LEU290 |
G | ARG298 |
G | PHE321 |
G | ALA348 |
G | PHE349 |
G | GLY350 |
G | ALA353 |
G | HIS354 |
G | HIS355 |
G | CYS356 |
G | ILE357 |
G | DEB502 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue DEB G 502 |
Chain | Residue |
G | PHE84 |
G | LEU94 |
G | ILE243 |
G | GLY294 |
G | SER295 |
G | PHE296 |
G | HEM501 |
site_id | AD6 |
Number of Residues | 21 |
Details | binding site for residue HEM H 501 |
Chain | Residue |
H | VAL93 |
H | LEU94 |
H | HIS101 |
H | ARG105 |
H | LEU241 |
H | ALA244 |
H | GLY245 |
H | THR248 |
H | GLN252 |
H | ARG298 |
H | ALA348 |
H | PHE349 |
H | GLY350 |
H | HIS354 |
H | CYS356 |
H | ILE357 |
H | GLY358 |
H | LEU361 |
H | GLU365 |
H | DEB502 |
H | HOH602 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue DEB H 502 |
Chain | Residue |
H | PHE84 |
H | ILE243 |
H | ALA244 |
H | SER295 |
H | LEU396 |
H | HEM501 |
H | HOH602 |
site_id | AD8 |
Number of Residues | 13 |
Details | binding site for residue HEM I 501 |
Chain | Residue |
I | VAL93 |
I | LEU94 |
I | HIS101 |
I | ARG105 |
I | ALA244 |
I | GLY245 |
I | THR248 |
I | LEU285 |
I | HIS354 |
I | CYS356 |
I | ILE357 |
I | LEU361 |
I | DEB502 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for residue DEB I 502 |
Chain | Residue |
I | PHE84 |
I | LEU94 |
I | LEU179 |
I | SER240 |
I | ALA244 |
I | THR248 |
I | LEU396 |
I | HEM501 |
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 |