3MVR
Crystal Structure of cytochrome P450 2B4-H226Y in a closed conformation
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 | 0006082 | biological_process | organic acid metabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0008392 | molecular_function | arachidonate epoxygenase activity |
| A | 0016491 | molecular_function | oxidoreductase 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 |
| 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 | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006082 | biological_process | organic acid metabolic process |
| B | 0006805 | biological_process | xenobiotic metabolic process |
| B | 0008392 | molecular_function | arachidonate epoxygenase activity |
| B | 0016491 | molecular_function | oxidoreductase 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 |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | ARG98 |
| A | GLN357 |
| A | ILE363 |
| A | VAL367 |
| A | HIS369 |
| A | LEU392 |
| A | PRO428 |
| A | PHE429 |
| A | SER430 |
| A | ARG434 |
| A | CYS436 |
| A | ILE114 |
| A | LEU437 |
| A | GLY438 |
| A | ILE441 |
| A | ALA442 |
| A | HOH993 |
| A | TRP121 |
| A | ARG125 |
| A | ALA298 |
| A | GLY299 |
| A | THR302 |
| A | THR303 |
| A | THR306 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CM5 A 601 |
| Chain | Residue |
| A | LYS186 |
| A | PHE188 |
| A | PHE195 |
| A | PHE202 |
| A | PHE244 |
| A | LYS251 |
| A | GLU466 |
| A | ASP467 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CM5 A 602 |
| Chain | Residue |
| A | LEU43 |
| A | LEU44 |
| A | MET46 |
| A | ASP47 |
| A | ARG48 |
| A | GLN215 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM B 500 |
| Chain | Residue |
| B | ARG98 |
| B | ILE114 |
| B | TRP121 |
| B | ARG125 |
| B | ALA298 |
| B | GLY299 |
| B | THR302 |
| B | THR303 |
| B | THR306 |
| B | GLN357 |
| B | ILE363 |
| B | VAL367 |
| B | HIS369 |
| B | LEU392 |
| B | PRO428 |
| B | PHE429 |
| B | SER430 |
| B | ARG434 |
| B | CYS436 |
| B | GLY438 |
| B | ILE441 |
| B | ALA442 |
| B | HOH778 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CM5 B 603 |
| Chain | Residue |
| B | LEU43 |
| B | LEU44 |
| B | MET46 |
| B | ASP47 |
| B | GLY50 |
| B | GLN215 |
| B | VAL216 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CM5 B 604 |
| Chain | Residue |
| B | LYS186 |
| B | PHE188 |
| B | ASP192 |
| B | VAL194 |
| B | PHE195 |
| B | LEU198 |
| B | PHE244 |
| B | LYS251 |
| B | PHE296 |
| B | ASP467 |
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 | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P00176","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
