5GWE
cytochrome P450 CREJ
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | binding site for residue HEM A 501 |
Chain | Residue |
A | PHE98 |
A | THR296 |
A | THR297 |
A | TRP342 |
A | ARG344 |
A | MET367 |
A | SER395 |
A | PHE396 |
A | PHE398 |
A | HIS401 |
A | CYS403 |
A | LEU135 |
A | GLY405 |
A | ALA409 |
A | GWM502 |
A | HOH639 |
A | HOH671 |
A | HOH679 |
A | SER136 |
A | HIS143 |
A | ARG147 |
A | PHE154 |
A | SER288 |
A | ALA292 |
A | GLY293 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue GWM A 502 |
Chain | Residue |
A | GLN110 |
A | SER133 |
A | GLY134 |
A | LEU135 |
A | SER136 |
A | ARG221 |
A | SER288 |
A | PHE291 |
A | ALA292 |
A | ILE339 |
A | TRP342 |
A | HEM501 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | PHE65 |
A | ARG306 |
A | TYR335 |
A | ARG372 |
A | ARG444 |
A | HOH625 |
A | HOH673 |
A | HOH843 |
A | HOH866 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | ARG147 |
A | GLN151 |
A | HOH609 |
A | HOH802 |
A | HOH877 |
A | HOH959 |
A | HOH962 |
site_id | AC5 |
Number of Residues | 28 |
Details | binding site for residue HEM B 501 |
Chain | Residue |
B | PHE98 |
B | LEU135 |
B | SER136 |
B | HIS143 |
B | ARG147 |
B | ILE200 |
B | SER288 |
B | ALA292 |
B | GLY293 |
B | THR296 |
B | THR297 |
B | LEU300 |
B | TRP342 |
B | ARG344 |
B | MET367 |
B | SER395 |
B | PHE396 |
B | GLY397 |
B | PHE398 |
B | HIS401 |
B | CYS403 |
B | LEU404 |
B | GLY405 |
B | ALA409 |
B | GWM502 |
B | HOH648 |
B | HOH668 |
B | HOH715 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue GWM B 502 |
Chain | Residue |
B | GLN110 |
B | SER133 |
B | GLY134 |
B | LEU135 |
B | SER136 |
B | ARG221 |
B | SER288 |
B | PHE291 |
B | ALA292 |
B | ILE339 |
B | TRP342 |
B | HEM501 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 503 |
Chain | Residue |
B | HOH693 |
B | HOH714 |
B | ASN63 |
B | PHE65 |
B | ARG306 |
B | TYR335 |
B | ARG372 |
B | ARG444 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 504 |
Chain | Residue |
B | ARG114 |
B | HOH609 |
B | HOH682 |
D | ARG147 |
D | GLN151 |
D | HOH678 |
site_id | AC9 |
Number of Residues | 28 |
Details | binding site for residue HEM C 501 |
Chain | Residue |
C | PHE98 |
C | LEU135 |
C | SER136 |
C | HIS143 |
C | ARG147 |
C | PHE154 |
C | ILE200 |
C | SER288 |
C | ALA292 |
C | GLY293 |
C | THR296 |
C | THR297 |
C | LEU300 |
C | TRP342 |
C | ARG344 |
C | MET367 |
C | SER395 |
C | PHE396 |
C | GLY397 |
C | PHE398 |
C | HIS401 |
C | CYS403 |
C | GLY405 |
C | ALA409 |
C | GWM502 |
C | HOH657 |
C | HOH725 |
C | HOH751 |
site_id | AD1 |
Number of Residues | 12 |
Details | binding site for residue GWM C 502 |
Chain | Residue |
C | GLN110 |
C | SER133 |
C | GLY134 |
C | LEU135 |
C | SER136 |
C | ARG221 |
C | SER288 |
C | PHE291 |
C | ALA292 |
C | ILE339 |
C | TRP342 |
C | HEM501 |
site_id | AD2 |
Number of Residues | 10 |
Details | binding site for residue SO4 C 503 |
Chain | Residue |
C | PHE65 |
C | ARG306 |
C | TYR335 |
C | ARG372 |
C | ARG444 |
C | HOH619 |
C | HOH764 |
C | HOH766 |
C | HOH769 |
C | HOH786 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue SO4 C 504 |
Chain | Residue |
C | ARG147 |
C | GLN151 |
C | HOH781 |
C | HOH837 |
C | HOH908 |
C | HOH913 |
site_id | AD4 |
Number of Residues | 25 |
Details | binding site for residue HEM D 501 |
Chain | Residue |
D | PHE98 |
D | LEU135 |
D | SER136 |
D | HIS143 |
D | ARG147 |
D | PHE154 |
D | ILE200 |
D | SER288 |
D | ALA292 |
D | GLY293 |
D | THR296 |
D | LEU300 |
D | ARG344 |
D | SER395 |
D | PHE396 |
D | PHE398 |
D | HIS401 |
D | CYS403 |
D | LEU404 |
D | GLY405 |
D | ALA409 |
D | GWM502 |
D | HOH629 |
D | HOH721 |
D | HOH731 |
site_id | AD5 |
Number of Residues | 12 |
Details | binding site for residue GWM D 502 |
Chain | Residue |
D | GLN110 |
D | SER133 |
D | GLY134 |
D | LEU135 |
D | SER136 |
D | ARG221 |
D | SER288 |
D | PHE291 |
D | ALA292 |
D | ILE339 |
D | TRP342 |
D | HEM501 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for residue SO4 D 503 |
Chain | Residue |
D | PHE65 |
D | ARG306 |
D | TYR335 |
D | ARG372 |
D | ARG444 |
D | HOH636 |
D | HOH749 |
D | HOH754 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGIHYCLG |
Chain | Residue | Details |
A | PHE396-GLY405 |