4JLT
Crystal structure of P450 2B4(H226Y) in complex with paroxetine
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | ARG98 |
| A | THR306 |
| A | ILE363 |
| A | VAL367 |
| A | HIS369 |
| A | PRO428 |
| A | PHE429 |
| A | SER430 |
| A | ARG434 |
| A | CYS436 |
| A | GLY438 |
| A | ILE114 |
| A | ALA442 |
| A | 8PR505 |
| A | HOH710 |
| A | HOH757 |
| A | HOH812 |
| A | TRP121 |
| A | ARG125 |
| A | ILE179 |
| A | ALA298 |
| A | GLY299 |
| A | THR302 |
| A | THR303 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CM5 A 502 |
| Chain | Residue |
| A | SER176 |
| A | PHE184 |
| A | LYS186 |
| A | PHE188 |
| A | PHE195 |
| A | PHE202 |
| A | PHE296 |
| A | GLU466 |
| A | PO4512 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CM5 A 503 |
| Chain | Residue |
| A | GLU250 |
| A | LEU269 |
| A | GLU273 |
| A | HIS285 |
| A | HIS319 |
| A | GLU322 |
| A | LEU489 |
| A | ALA490 |
| A | HOH719 |
| A | HOH775 |
| A | HOH776 |
| A | HOH806 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CM5 A 504 |
| Chain | Residue |
| A | LEU43 |
| A | LEU44 |
| A | MET46 |
| A | ASP47 |
| A | GLY50 |
| A | VAL216 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 8PR A 505 |
| Chain | Residue |
| A | ILE101 |
| A | ILE114 |
| A | PHE206 |
| A | GLU218 |
| A | PHE297 |
| A | GLU301 |
| A | PHE365 |
| A | GLY366 |
| A | VAL367 |
| A | VAL477 |
| A | HEM501 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 506 |
| Chain | Residue |
| A | LYS276 |
| A | ARG491 |
| A | HOH776 |
| A | HOH789 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 507 |
| Chain | Residue |
| A | HIS319 |
| A | ARG323 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 508 |
| Chain | Residue |
| A | ARG343 |
| A | ALA344 |
| A | HOH683 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 509 |
| Chain | Residue |
| A | THR404 |
| A | PRO405 |
| A | ASN406 |
| A | THR407 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 510 |
| Chain | Residue |
| A | ASP90 |
| A | GLN91 |
| A | ALA92 |
| A | GLU93 |
| A | ALA94 |
| A | LYS433 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 511 |
| Chain | Residue |
| A | SER213 |
| A | GLY229 |
| A | THR230 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 512 |
| Chain | Residue |
| A | SER248 |
| A | LYS251 |
| A | HIS252 |
| A | CM5502 |
| A | HOH797 |
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 | 1 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P00176","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
