PDBe 1j8t

X-ray diffraction
1.7Å resolution

Catalytic Domain of Human Phenylalanine Hydroxylase Fe(II)

Released:

Function and Biology Details

Reaction catalysed:
L-phenylalanine + tetrahydrobiopterin + O(2) = L-tyrosine + 4a-hydroxytetrahydrobiopterin
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine-4-hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 37.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00439 (Residues: 103-427; Coverage: 72%)
Gene name: PAH
Structure domains: Aromatic amino acid hydroxylase

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: C2221
Unit cell:
a: 66.334Å b: 108.419Å c: 124.024Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.252
Expression system: Escherichia coli