› 4anp

X-ray diffraction
2.11Å resolution

Crystal structure of human phenylalanine hydroxylase in complex with a pharmacological chaperone

Released:
DOI: 10.2210/pdb4anp/pdb
PDB entry 4anp coloured by chain, front view.
PDB entry 4anp coloured by chain, side view.
PDB entry 4anp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and mechanistic basis of the interaction between a pharmacological chaperone and human phenylalanine hydroxylase.
Torreblanca R, Lira-Navarrete E, Sancho J, Hurtado-Guerrero R
Chembiochem 13 1266-9 (2012)
PMID: 22549968

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 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: 324 amino acids
Theoretical weight: 37.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00439 (Residues: 104-427; Coverage: 72%)
Gene name: PAH
Sequence domains: Biopterin-dependent aromatic amino acid hydroxylase
Structure domains: Aromatic amino acid hydroxylase

Ligands and Environments

2 bound ligands:
Ligand FE 1 x FE
Ligand 3QI 1 x 3QI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER
Spacegroup: C2221
Unit cell:
a: 66.283Å b: 107.511Å c: 124.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Pharmacological chaperoning: a primer on mechanism and pharmacology.
Leidenheimer et al. (2014)
4 more

1 mention without citation

Molden 2.0: quantum chemistry meets proteins.
Schaftenaar et al. (2017)