› 1kw0

X-ray diffraction
2.5Å resolution

Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine

Released:
DOI: 10.2210/pdb1kw0/pdb
PDB entry 1kw0 coloured by chain, front view.
PDB entry 1kw0 coloured by chain, side view.
PDB entry 1kw0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its implications for the mechanism of catalysis and substrate activation.
Andersen OA, Flatmark T, Hough E
J Mol Biol 320 1095-108 (2002)
PMID: 12126628

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132487 (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
Sequence domains: Biopterin-dependent aromatic amino acid hydroxylase
Structure domains: Aromatic amino acid hydroxylase

Ligands and Environments


Cofactor: Ligand H4B 1 x H4B
2 bound ligands:
Ligand FE2 1 x FE2
Ligand TIH 1 x TIH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: C2221
Unit cell:
a: 65.172Å b: 106.741Å c: 123.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.267
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Tetrahydrobiopterin: biochemistry and pathophysiology.
Werner et al. (2011)
12 more

12 mentions without citation

Tyrosine hydroxylase and regulation of dopamine synthesis.
Daubner et al. (2011)
11 more