› 1dmw

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF DOUBLE TRUNCATED HUMAN PHENYLALANINE HYDROXYLASE WITH BOUND 7,8-DIHYDRO-L-BIOPTERIN

Released:
DOI: 10.2210/pdb1dmw/pdb
PDB entry 1dmw coloured by chain, front view.
PDB entry 1dmw coloured by chain, side view.
PDB entry 1dmw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase.
Erlandsen H, Bjørgo E, Flatmark T, Stevens RC
Biochemistry 39 2208-17 (2000)
PMID: 10694386

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: 307 amino acids
Theoretical weight: 35.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00439 (Residues: 118-424; Coverage: 68%)
Gene name: PAH
Sequence domains: Biopterin-dependent aromatic amino acid hydroxylase
Structure domains: Aromatic amino acid hydroxylase

Ligands and Environments


Cofactor: Ligand HBI 1 x HBI
1 bound ligand:
Ligand FE 1 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2221
Unit cell:
a: 66.357Å b: 107.991Å c: 124.591Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.246
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Non-heme iron oxygenases.
Ryle et al. (2002)
9 more

4 mentions without citation

Deamidation of human proteins.
Robinson et al. (2001)
3 more