3G93
Single 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 | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0008392 | molecular_function | arachidonate epoxygenase activity |
| 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 |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006805 | biological_process | xenobiotic metabolic process |
| B | 0008392 | molecular_function | arachidonate epoxygenase activity |
| 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 |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005789 | cellular_component | endoplasmic reticulum membrane |
| C | 0006805 | biological_process | xenobiotic metabolic process |
| C | 0008392 | molecular_function | arachidonate epoxygenase activity |
| 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 |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| D | 0006805 | biological_process | xenobiotic metabolic process |
| D | 0008392 | molecular_function | arachidonate epoxygenase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | ARG98 |
| A | HIS369 |
| A | PRO428 |
| A | PHE429 |
| A | SER430 |
| A | ARG434 |
| A | CYS436 |
| A | LEU437 |
| A | GLY438 |
| A | PB2501 |
| A | TRP121 |
| A | ARG125 |
| A | PHE296 |
| A | GLY299 |
| A | THR302 |
| A | THR303 |
| A | ILE363 |
| A | VAL367 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PB2 A 501 |
| Chain | Residue |
| A | ALA298 |
| A | GLY299 |
| A | THR302 |
| A | HEM500 |
| B | PHE217 |
| B | PHE223 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PB2 A 496 |
| Chain | Residue |
| A | PHE217 |
| A | PHE223 |
| A | LEU224 |
| B | ALA298 |
| B | GLY299 |
| B | THR302 |
| B | PRO368 |
| B | HEM500 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM B 500 |
| Chain | Residue |
| A | PHE217 |
| A | PB2496 |
| B | ARG98 |
| B | TRP121 |
| B | ARG125 |
| B | PHE296 |
| B | GLY299 |
| B | THR302 |
| B | THR303 |
| B | GLN357 |
| B | ILE363 |
| B | VAL367 |
| B | HIS369 |
| B | PRO428 |
| B | PHE429 |
| B | SER430 |
| B | ARG434 |
| B | CYS436 |
| B | GLY438 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM C 500 |
| Chain | Residue |
| C | ARG98 |
| C | ARG125 |
| C | PHE296 |
| C | GLY299 |
| C | THR300 |
| C | THR302 |
| C | THR303 |
| C | ILE363 |
| C | VAL367 |
| C | HIS369 |
| C | PRO428 |
| C | PHE429 |
| C | SER430 |
| C | ARG434 |
| C | CYS436 |
| C | GLY438 |
| C | ALA442 |
| C | PB2501 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PB2 C 501 |
| Chain | Residue |
| C | ALA298 |
| C | GLY299 |
| C | THR302 |
| C | ILE363 |
| C | HEM500 |
| D | PHE217 |
| D | PHE223 |
| D | LEU224 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM D 500 |
| Chain | Residue |
| D | ARG98 |
| D | TRP121 |
| D | ARG125 |
| D | PHE296 |
| D | GLY299 |
| D | THR300 |
| D | THR302 |
| D | THR303 |
| D | THR306 |
| D | GLN357 |
| D | ILE363 |
| D | VAL367 |
| D | HIS369 |
| D | LEU392 |
| D | PRO428 |
| D | PHE429 |
| D | SER430 |
| D | ARG434 |
| D | CYS436 |
| D | LEU437 |
| D | GLY438 |
| D | PB2501 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PB2 D 501 |
| Chain | Residue |
| C | PHE217 |
| C | PHE223 |
| C | LEU224 |
| D | ALA298 |
| D | GLY299 |
| D | THR302 |
| D | ILE363 |
| D | HEM500 |
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 site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P00176","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
