3EL3
Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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: axial binding residue => ECO:0000269|PubMed:19858213 |
Chain | Residue | Details |
A | CYS410 | |
B | CYS410 |