1PHZ
STRUCTURE OF PHOSPHORYLATED PHENYLALANINE HYDROXYLASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0004505 | molecular_function | phenylalanine 4-monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006558 | biological_process | L-phenylalanine metabolic process |
| A | 0006559 | biological_process | L-phenylalanine catabolic process |
| A | 0006571 | biological_process | tyrosine biosynthetic process |
| A | 0008152 | biological_process | metabolic process |
| A | 0009072 | biological_process | aromatic amino acid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016597 | molecular_function | amino acid binding |
| 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 |
| A | 0019293 | biological_process | tyrosine biosynthetic process, by oxidation of phenylalanine |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 501 |
| Chain | Residue |
| A | HIS285 |
| A | HIS290 |
| A | GLU330 |
| A | HOH533 |
| site_id | FE |
| Number of Residues | 3 |
| Details | IRON BINDING SITE |
| Chain | Residue |
| A | HIS285 |
| A | HIS290 |
| A | GLU330 |
Functional Information from PROSITE/UniProt
| site_id | PS00367 |
| Number of Residues | 12 |
| Details | BH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDicHELLGHVP |
| Chain | Residue | Details |
| A | PRO281-PRO292 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10331871, ECO:0007744|PDB:1PHZ, ECO:0007744|PDB:2PHM |
| Chain | Residue | Details |
| A | HIS285 | |
| A | HIS290 | |
| A | GLU330 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P16331 |
| Chain | Residue | Details |
| A | ALA2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:7387651, ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| A | SER16 |
