Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009808 | biological_process | lignin metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016710 | molecular_function | trans-cinnamate 4-monooxygenase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue EPE A 601 |
| Chain | Residue |
| A | PHE107 |
| A | HOH938 |
| A | HOH1085 |
| A | ARG213 |
| A | SER214 |
| A | SER217 |
| A | GLN218 |
| A | VAL301 |
| A | ALA302 |
| A | ILE367 |
| A | HEM602 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue HEM A 602 |
| Chain | Residue |
| A | ARG101 |
| A | VAL118 |
| A | TRP126 |
| A | ARG130 |
| A | PHE138 |
| A | MET186 |
| A | ALA302 |
| A | ALA303 |
| A | THR307 |
| A | LEU370 |
| A | VAL371 |
| A | HIS373 |
| A | PRO435 |
| A | PHE436 |
| A | ARG441 |
| A | CYS443 |
| A | PRO444 |
| A | GLY445 |
| A | LEU448 |
| A | ALA449 |
| A | EPE601 |
| A | HOH765 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 603 |
| Chain | Residue |
| A | LEU47 |
| A | GLN48 |
| A | VAL49 |
| A | HOH705 |
| A | HOH705 |
| A | HOH962 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 604 |
| Chain | Residue |
| A | THR102 |
| A | ARG103 |
| A | PHE107 |
| A | PHE119 |
| A | LYS391 |
| A | HOH750 |
| A | HOH872 |
| A | HOH909 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGvGRRSCPG |
| Chain | Residue | Details |
| A | PHE436-GLY445 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32332088","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"32332088","evidenceCode":"ECO:0000269"}]} |
