Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009072 | biological_process | aromatic amino acid metabolic process |
| A | 0016714 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 501 |
| Chain | Residue |
| A | HOH602 |
| A | HIS331 |
| A | HIS336 |
| A | GLU376 |
| A | HBI500 |
| A | HOH601 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 510 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HBI A 500 |
| Chain | Residue |
| A | LEU294 |
| A | LEU295 |
| A | MTY300 |
| A | GLN310 |
| A | PRO327 |
| A | GLU332 |
| A | TYR371 |
| A | GLU376 |
| A | FE501 |
| A | HOH603 |
| site_id | FE |
| Number of Residues | 3 |
| Details | IRON BINDING SITE. |
| Chain | Residue |
| A | HIS331 |
| A | HIS336 |
| A | GLU376 |
| site_id | MTY |
| Number of Residues | 1 |
| Details | PTERIN BINDING SITE AND SELF-HYDROXYLATED RESIDUE |
Functional Information from PROSITE/UniProt
| site_id | PS00367 |
| Number of Residues | 12 |
| Details | BH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDccHELLGHVP |
| Chain | Residue | Details |
| A | PRO327-PRO338 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS331 | |
| A | HIS336 | |
| A | GLU376 | |
| Chain | Residue | Details |
| A | ASP425 | |
| Chain | Residue | Details |
| A | SER472 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 14640675, 10747809 |
| Chain | Residue | Details |
| A | SER395 | |
| A | HIS331 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 134 |
| Chain | Residue | Details |
| A | HIS331 | electrostatic stabiliser, hydrogen bond donor, metal ligand |
| A | HIS336 | metal ligand |
| A | GLU376 | metal ligand |
| A | SER395 | electrostatic stabiliser, hydrogen bond acceptor, steric role |
