› 1ltz

X-ray diffraction
1.4Å resolution

CRYSTAL STRUCTURE OF CHROMOBACTERIUM VIOLACEUM PHENYLALANINE HYDROXYLASE, STRUCTURE HAS BOUND IRON (III) AND OXIDIZED COFACTOR 7,8-DIHYDROBIOPTERIN

Released:
DOI: 10.2210/pdb1ltz/pdb
PDB entry 1ltz coloured by chain, front view.
PDB entry 1ltz coloured by chain, side view.
PDB entry 1ltz coloured by chain, top view.
Source organism: Chromobacterium violaceum
Primary publication:
Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates.
Erlandsen H, Kim JY, Patch MG, Han A, Volner A, Abu-Omar MM, Stevens RC
J Mol Biol 320 645-61 (2002)
PMID: 12096915

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-151852 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine-4-hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 33.63 KDa
Source organism: Chromobacterium violaceum
Expression system: Escherichia coli
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


Cofactor: Ligand HBI 1 x HBI
2 bound ligands:
Ligand FE 1 x FE
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 46.7Å b: 67.86Å c: 91.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.159 0.223
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes.
Koehntop et al. (2005)
7 more

5 mentions without citation

Dynamic regulation of phenylalanine hydroxylase by simulated redox manipulation.
Fuchs et al. (2012)
4 more