X-ray diffraction
1.5Å resolution

Biochemical properties and crystal structure of a novel beta- phenylalanine aminotransferase from Variovorax paradoxus


Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Beta-phenylalanine transaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 454 amino acids
Theoretical weight: 48.63 KDa
Source organism: Variovorax paradoxus
Expression system: Escherichia coli
  • Canonical: H8WR05 (Residues: 1-434; Coverage: 100%)
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 88.74Å b: 100.11Å c: 104.799Å
α: 90° β: 90° γ: 90°
R R work R free
0.168 0.167 0.182
Expression system: Escherichia coli