› 1tdw

X-ray diffraction
2.1Å resolution

Crystal structure of double truncated human phenylalanine hydroxylase BH4-responsive PKU mutant A313T.

Released:
DOI: 10.2210/pdb1tdw/pdb
PDB entry 1tdw coloured by chain, front view.
PDB entry 1tdw coloured by chain, side view.
PDB entry 1tdw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations.
Erlandsen H, Pey AL, Gámez A, Pérez B, Desviat LR, Aguado C, Koch R, Surendran S, Tyring S, Matalon R, Scriver CR, Ugarte M, Martínez A, Stevens RC
Proc Natl Acad Sci U S A 101 16903-8 (2004)
PMID: 15557004

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: 35.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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: RIGAKU FR-D
Spacegroup: C2221
Unit cell:
a: 66.411Å b: 108.138Å c: 124.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

22 review citations

B6-responsive disorders: a model of vitamin dependency.
Clayton PT. (2006)
21 more

2 mentions without citation

Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations.
Erlandsen et al. (2004)
1 more