6BWW
Crystal structure of an acetate and Cymal-5 bound cytochrome P450 2B4 F429H mutant
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 | arachidonic acid 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 |
A | 0070330 | molecular_function | aromatase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | binding site for residue HEM A 501 |
Chain | Residue |
A | ARG98 |
A | THR303 |
A | THR306 |
A | GLN357 |
A | ILE363 |
A | VAL367 |
A | HIS369 |
A | LEU392 |
A | PRO428 |
A | HIS429 |
A | SER430 |
A | VAL113 |
A | ARG434 |
A | CYS436 |
A | LEU437 |
A | GLY438 |
A | ALA442 |
A | ACT504 |
A | HOH716 |
A | ILE114 |
A | TRP121 |
A | ARG125 |
A | ILE179 |
A | ALA298 |
A | GLY299 |
A | THR302 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue CM5 A 502 |
Chain | Residue |
A | LYS186 |
A | PHE188 |
A | LEU198 |
A | PHE244 |
A | LYS251 |
A | PHE296 |
A | ACT506 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue CM5 A 503 |
Chain | Residue |
A | ILE101 |
A | ILE114 |
A | PHE115 |
A | PHE297 |
A | PHE365 |
A | GLY366 |
A | PRO368 |
A | GLY476 |
A | VAL477 |
A | HOH617 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ACT A 504 |
Chain | Residue |
A | ALA298 |
A | THR302 |
A | ILE363 |
A | HEM501 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue ACT A 505 |
Chain | Residue |
A | ILE468 |
A | ASP469 |
A | PRO482 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue ACT A 506 |
Chain | Residue |
A | LYS186 |
A | PHE244 |
A | SER248 |
A | LYS251 |
A | HIS252 |
A | CM5502 |
A | GOL514 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue ACT A 507 |
Chain | Residue |
A | SER96 |
A | ASN117 |
A | GLY118 |
A | THR372 |
A | ARG434 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue ACT A 508 |
Chain | Residue |
A | PHE135 |
A | MET137 |
A | ARG145 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue ACT A 509 |
Chain | Residue |
A | PHE244 |
A | GLN247 |
A | SER248 |
A | LYS251 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue ACT A 510 |
Chain | Residue |
A | ARG125 |
A | LEU129 |
A | ARG133 |
A | HOH602 |
A | HOH607 |
A | HOH789 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue ACT A 511 |
Chain | Residue |
A | ARG323 |
A | HOH675 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue GOL A 512 |
Chain | Residue |
A | PHE426 |
A | MET427 |
A | PRO428 |
A | HIS429 |
A | SER430 |
A | ILE435 |
A | GLU439 |
A | HOH612 |
A | HOH631 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue GOL A 513 |
Chain | Residue |
A | LYS316 |
A | TYR317 |
A | PRO465 |
A | GLU466 |
A | HOH619 |
A | HOH704 |
A | HOH878 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 514 |
Chain | Residue |
A | PHE184 |
A | GLY185 |
A | LYS251 |
A | HIS252 |
A | ACT506 |
A | HOH741 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 515 |
Chain | Residue |
A | ARG197 |
A | GLU240 |
A | THR243 |
A | PHE244 |
A | GLN247 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue GOL A 516 |
Chain | Residue |
A | ASP82 |
A | ARG85 |
A | GLU86 |
A | ASP90 |
A | HOH626 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue GOL A 517 |
Chain | Residue |
A | HIS354 |
A | LYS421 |
A | ARG422 |
A | ASN423 |
A | PHE426 |
A | HOH601 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | CYS436 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P00176 |
Chain | Residue | Details |
A | SER128 |