4q3x

X-ray diffraction
1.35Å resolution

Crystal structure of C. violaceum phenylalanine hydroxylase D139N mutation

Released:

Function and Biology Details

Reaction catalysed:
L-phenylalanine + tetrahydrobiopterin + O(2) = L-tyrosine + 4a-hydroxytetrahydrobiopterin
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine-4-hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 33.65 KDa
Source organism: Chromobacterium violaceum ATCC 12472
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30967 (Residues: 1-297; Coverage: 100%)
Gene names: CV_3180, phhA
Sequence domains: Biopterin-dependent aromatic amino acid hydroxylase
Structure domains: Aromatic amino acid hydroxylase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P1
Unit cell:
a: 36.804Å b: 38.534Å c: 47.818Å
α: 76.53° β: 73.09° γ: 85.55°
R-values:
R R work R free
0.162 0.161 0.2
Expression system: Escherichia coli BL21(DE3)