3EL3
Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0010333 | molecular_function | terpene synthase activity |
| A | 0010334 | molecular_function | sesquiterpene synthase 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 | 0016829 | molecular_function | lyase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0020037 | molecular_function | heme binding |
| A | 0042181 | biological_process | ketone biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051762 | biological_process | sesquiterpene biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0010333 | molecular_function | terpene synthase activity |
| B | 0010334 | molecular_function | sesquiterpene synthase 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 | 0016829 | molecular_function | lyase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0020037 | molecular_function | heme binding |
| B | 0042181 | biological_process | ketone biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051762 | biological_process | sesquiterpene biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | ASN108 |
| A | ARG408 |
| A | LYS409 |
| A | CYS410 |
| A | SER412 |
| A | SER416 |
| A | ILE271 |
| A | GLY275 |
| A | THR278 |
| A | ILE279 |
| A | THR282 |
| A | ARG343 |
| A | PRO402 |
| A | PHE403 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EL3 A 501 |
| Chain | Residue |
| A | TRP92 |
| A | PRO274 |
| A | VAL338 |
| A | ILE447 |
| A | THR448 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EL3 A 502 |
| Chain | Residue |
| A | LEU91 |
| A | TRP339 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 500 |
| Chain | Residue |
| B | ASN108 |
| B | ILE271 |
| B | GLY275 |
| B | THR278 |
| B | ILE279 |
| B | THR282 |
| B | LEU341 |
| B | ARG343 |
| B | PRO402 |
| B | SER404 |
| B | LYS407 |
| B | ARG408 |
| B | LYS409 |
| B | CYS410 |
| B | SER412 |
| B | SER416 |
| B | EL3501 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EL3 B 501 |
| Chain | Residue |
| B | TRP92 |
| B | THR278 |
| B | VAL338 |
| B | ILE447 |
| B | THR448 |
| B | HEM500 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EL3 B 502 |
| Chain | Residue |
| B | LEU91 |
| B | TRP339 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"19858213","evidenceCode":"ECO:0000269"}]} |
| 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 | THR278 | |
| A | GLU277 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| B | THR278 | |
| B | GLU277 |
