› 1pah

X-ray diffraction
2Å resolution

HUMAN PHENYLALANINE HYDROXYLASE DIMER, RESIDUES 117-424

Released:
DOI: 10.2210/pdb1pah/pdb
PDB entry 1pah coloured by chain, front view.
PDB entry 1pah coloured by chain, side view.
PDB entry 1pah coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria.
Erlandsen H, Fusetti F, Martinez A, Hough E, Flatmark T, Stevens RC
Nat Struct Biol 4 995-1000 (1997)
PMID: 9406548

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132486 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine-4-hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 308 amino acids
Theoretical weight: 35.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00439 (Residues: 117-424; Coverage: 68%)
Gene name: PAH
Sequence domains: Biopterin-dependent aromatic amino acid hydroxylase
Structure domains: Aromatic amino acid hydroxylase

Ligands and Environments

1 bound ligand:
Ligand FE 1 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: C2221
Unit cell:
a: 66.6Å b: 108.4Å c: 125.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.218
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Tetrahydropterin-dependent amino acid hydroxylases.
Fitzpatrick PF. (1999)
18 more

9 mentions without citation

Structural insights into the regulation of aromatic amino acid hydroxylation.
Fitzpatrick PF. (2015)
8 more