1mmk

X-ray diffraction
2Å resolution

Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase ((FeII)) complexed with tetrahydrobiopterin and thienylalanine

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (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
Structure domains: Aromatic amino acid hydroxylase

Ligands and Environments


Cofactor: Ligand H4B 1 x H4B
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2221
Unit cell:
a: 65.194Å b: 107.86Å c: 123.437Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.229
Expression system: Escherichia coli