› 1mmt

X-ray diffraction
2Å resolution

Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase (Fe(II)) complexed with tetrahydrobiopterin and norleucine

Released:
DOI: 10.2210/pdb1mmt/pdb
PDB entry 1mmt coloured by chain, front view.
PDB entry 1mmt coloured by chain, side view.
PDB entry 1mmt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding.
Andersen OA, Stokka AJ, Flatmark T, Hough E
J Mol Biol 333 747-57 (2003)
PMID: 14568534

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
3 bound ligands:
Ligand FE2 1 x FE2
Ligand SO4 1 x SO4
Ligand NLE 1 x NLE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: C2221
Unit cell:
a: 65.14Å b: 106.638Å c: 123.611Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.243
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Versatility of biological non-heme Fe(II) centers in oxygen activation reactions.
Kovaleva et al. (2008)
7 more

8 mentions without citation

New protein structures provide an updated understanding of phenylketonuria.
Jaffe EK. (2017)
7 more