PDBe 2toh

X-ray diffraction
2.3Å resolution

TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine 3-monooxygenase Chain: A
Molecule details ›
Chain: A
Length: 343 amino acids
Theoretical weight: 39.29 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04177 (Residues: 156-498; Coverage: 69%)
Gene name: Th
Sequence domains: Biopterin-dependent aromatic amino acid hydroxylase
Structure domains: Phenylalanine Hydroxylase

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: F222
Unit cell:
a: 189.464Å b: 148.595Å c: 56.986Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.276
Expression system: Escherichia coli