2RFB
Crystal Structure of a Cytochrome P450 from the Thermoacidophilic Archaeon Picrophilus Torridus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| 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 | 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 | 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 | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016491 | molecular_function | oxidoreductase 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 | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 900 |
| Chain | Residue |
| A | ASP99 |
| A | PHE325 |
| A | LYS326 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 910 |
| Chain | Residue |
| A | PHE280 |
| A | ASP281 |
| A | ARG290 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 920 |
| Chain | Residue |
| A | ILE54 |
| A | SER55 |
| A | LYS189 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 910 |
| Chain | Residue |
| C | PHE280 |
| C | ASP281 |
| C | ARG290 |
| C | ARG291 |
| C | HOH931 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 410 |
| Chain | Residue |
| A | PHE56 |
| A | ILE57 |
| A | HIS64 |
| A | ARG68 |
| A | LEU194 |
| A | GLY197 |
| A | GLY198 |
| A | THR201 |
| A | ILE241 |
| A | ARG247 |
| A | LEU270 |
| A | ALA296 |
| A | PHE297 |
| A | GLY298 |
| A | ILE301 |
| A | HIS302 |
| A | CYS304 |
| A | GLY306 |
| A | HOH944 |
| A | HOH946 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM B 410 |
| Chain | Residue |
| B | PHE56 |
| B | ILE57 |
| B | HIS64 |
| B | ARG68 |
| B | PHE75 |
| B | LEU193 |
| B | LEU194 |
| B | GLY197 |
| B | GLY198 |
| B | THR201 |
| B | HIS246 |
| B | ARG247 |
| B | LEU270 |
| B | ALA296 |
| B | PHE297 |
| B | GLY298 |
| B | ILE301 |
| B | HIS302 |
| B | CYS304 |
| B | GLY306 |
| B | LEU309 |
| B | ALA310 |
| B | HOH412 |
| B | HOH419 |
| B | HOH420 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM C 410 |
| Chain | Residue |
| C | PHE56 |
| C | ILE57 |
| C | HIS64 |
| C | ARG68 |
| C | LEU194 |
| C | GLY197 |
| C | GLY198 |
| C | THR201 |
| C | LEU205 |
| C | LEU235 |
| C | LEU244 |
| C | ARG247 |
| C | ALA296 |
| C | PHE297 |
| C | GLY298 |
| C | ILE301 |
| C | HIS302 |
| C | CYS304 |
| C | GLY306 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGiGIHMCLG |
| Chain | Residue | Details |
| A | PHE297-GLY306 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | THR201 | |
| A | GLU200 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| B | THR201 | |
| B | GLU200 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| C | THR201 | |
| C | GLU200 |
