3G5N
Triple ligand occupancy crystal structure of cytochrome P450 2B4 in complex with the inhibitor 1-biphenyl-4-methyl-1H-imidazole
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0008392 | molecular_function | arachidonate epoxygenase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| A | 0019373 | biological_process | epoxygenase P450 pathway |
| A | 0020037 | molecular_function | heme binding |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006805 | biological_process | xenobiotic metabolic process |
| B | 0008392 | molecular_function | arachidonate epoxygenase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| B | 0019373 | biological_process | epoxygenase P450 pathway |
| B | 0020037 | molecular_function | heme binding |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005789 | cellular_component | endoplasmic reticulum membrane |
| C | 0006805 | biological_process | xenobiotic metabolic process |
| C | 0008392 | molecular_function | arachidonate epoxygenase activity |
| C | 0016020 | cellular_component | membrane |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| C | 0019373 | biological_process | epoxygenase P450 pathway |
| C | 0020037 | molecular_function | heme binding |
| C | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| D | 0006805 | biological_process | xenobiotic metabolic process |
| D | 0008392 | molecular_function | arachidonate epoxygenase activity |
| D | 0016020 | cellular_component | membrane |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| D | 0019373 | biological_process | epoxygenase P450 pathway |
| D | 0020037 | molecular_function | heme binding |
| D | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | ARG98 |
| A | ILE363 |
| A | VAL367 |
| A | HIS369 |
| A | PRO428 |
| A | PHE429 |
| A | SER430 |
| A | ARG434 |
| A | CYS436 |
| A | LEU437 |
| A | GLY438 |
| A | TRP121 |
| A | PB2501 |
| A | HOH525 |
| A | ARG125 |
| A | PHE296 |
| A | GLY299 |
| A | THR300 |
| A | THR302 |
| A | THR303 |
| A | GLN357 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PB2 A 501 |
| Chain | Residue |
| A | ALA298 |
| A | GLY299 |
| A | THR302 |
| A | VAL367 |
| A | HEM500 |
| B | PHE217 |
| B | PHE223 |
| B | LYS225 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PB2 A 503 |
| Chain | Residue |
| A | LEU70 |
| A | ARG73 |
| A | GLU387 |
| B | ILE101 |
| B | PHE223 |
| B | LEU224 |
| B | PB2502 |
| B | HOH525 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CM5 A 504 |
| Chain | Residue |
| A | ARG98 |
| A | ILE114 |
| A | ASN117 |
| A | TRP121 |
| A | LEU288 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PB2 B 502 |
| Chain | Residue |
| A | TYR69 |
| A | LEU70 |
| A | VAL477 |
| A | PB2503 |
| B | LEU224 |
| B | LYS225 |
| B | PRO228 |
| B | THR230 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM B 500 |
| Chain | Residue |
| B | ARG98 |
| B | TRP121 |
| B | ARG125 |
| B | PHE296 |
| B | GLY299 |
| B | THR300 |
| B | THR302 |
| B | THR303 |
| B | THR306 |
| B | GLN357 |
| B | ILE363 |
| B | VAL367 |
| B | HIS369 |
| B | PRO428 |
| B | PHE429 |
| B | SER430 |
| B | ARG434 |
| B | CYS436 |
| B | LEU437 |
| B | GLY438 |
| B | HOH499 |
| B | PB2501 |
| B | HOH520 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PB2 B 501 |
| Chain | Residue |
| A | PHE217 |
| A | PHE223 |
| B | ALA298 |
| B | GLY299 |
| B | THR302 |
| B | VAL367 |
| B | PRO368 |
| B | HEM500 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PB2 B 496 |
| Chain | Residue |
| A | LYS225 |
| A | PHE227 |
| A | PRO228 |
| B | LEU43 |
| B | LEU51 |
| B | TYR69 |
| B | LEU70 |
| B | PRO368 |
| B | PHE389 |
| B | VAL477 |
| B | PB2503 |
| B | HOH535 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PB2 B 503 |
| Chain | Residue |
| A | LEU224 |
| B | ARG73 |
| B | GLU387 |
| B | PB2496 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CM5 B 504 |
| Chain | Residue |
| B | ILE114 |
| B | ASN117 |
| B | ARG120 |
| B | LEU288 |
| A | PHE220 |
| B | ARG98 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM C 500 |
| Chain | Residue |
| C | ARG98 |
| C | TRP121 |
| C | ARG125 |
| C | PHE296 |
| C | GLY299 |
| C | THR302 |
| C | THR303 |
| C | ILE363 |
| C | VAL367 |
| C | HIS369 |
| C | PRO428 |
| C | PHE429 |
| C | SER430 |
| C | ARG434 |
| C | CYS436 |
| C | LEU437 |
| C | GLY438 |
| C | PB2501 |
| C | HOH510 |
| D | PHE220 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PB2 C 501 |
| Chain | Residue |
| C | ALA298 |
| C | GLY299 |
| C | THR302 |
| C | VAL367 |
| C | PRO368 |
| C | HEM500 |
| D | PHE217 |
| D | PHE223 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PB2 C 502 |
| Chain | Residue |
| C | LEU43 |
| C | LEU51 |
| C | TYR69 |
| C | LEU70 |
| C | VAL477 |
| C | PB2503 |
| D | LEU224 |
| D | LYS225 |
| D | PHE227 |
| D | PRO228 |
| D | THR230 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PB2 C 503 |
| Chain | Residue |
| C | ARG73 |
| C | GLU387 |
| C | PB2502 |
| D | PHE223 |
| D | LEU224 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CM5 D 504 |
| Chain | Residue |
| C | VAL39 |
| D | ARG98 |
| D | ASN117 |
| D | TRP121 |
| D | LEU288 |
| D | HOH513 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CM5 C 504 |
| Chain | Residue |
| C | ARG98 |
| C | ILE114 |
| C | ASN117 |
| C | LEU288 |
| D | PHE220 |
| site_id | BC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM D 500 |
| Chain | Residue |
| D | ARG98 |
| D | TRP121 |
| D | ARG125 |
| D | PHE296 |
| D | GLY299 |
| D | THR302 |
| D | THR303 |
| D | ILE363 |
| D | VAL367 |
| D | HIS369 |
| D | PRO428 |
| D | PHE429 |
| D | SER430 |
| D | ARG434 |
| D | CYS436 |
| D | LEU437 |
| D | GLY438 |
| D | PB2501 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PB2 D 501 |
| Chain | Residue |
| C | PHE217 |
| C | PHE223 |
| D | ALA298 |
| D | GLY299 |
| D | THR302 |
| D | VAL367 |
| D | PRO368 |
| D | HEM500 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PB2 D 502 |
| Chain | Residue |
| C | PRO228 |
| C | THR230 |
| D | LEU43 |
| D | TYR69 |
| D | LEU70 |
| D | PHE365 |
| D | VAL477 |
| D | PB2503 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PB2 D 503 |
| Chain | Residue |
| C | LEU224 |
| D | LEU70 |
| D | ARG73 |
| D | GLU387 |
| D | PHE389 |
| D | PB2502 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSlGKRICLG |
| Chain | Residue | Details |
| A | PHE429-GLY438 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | GLN455 | |
| B | GLN455 | |
| C | GLN455 | |
| D | GLN455 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P00176 |
| Chain | Residue | Details |
| A | GLN147 | |
| B | GLN147 | |
| C | GLN147 | |
| D | GLN147 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | THR302 | |
| A | GLU301 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| B | THR302 | |
| B | GLU301 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| C | THR302 | |
| C | GLU301 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| D | THR302 | |
| D | GLU301 |
