X-ray diffraction
1.9Å resolution

Structural Investigations into the Stereochemistry and Activity of a Phenylalanine-2,3-Aminomutase from Taxus chinensis


Function and Biology Details

Reactions catalysed:
L-phenylalanine = trans-cinnamate + ammonia
L-phenylalanine = L-beta-phenylalanine
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Phenylalanine aminomutase (L-beta-phenylalanine forming) Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 705 amino acids
Theoretical weight: 77.46 KDa
Source organism: Taxus chinensis
Expression system: Escherichia coli
  • Canonical: Q68G84 (Residues: 1-687; Coverage: 100%)
Gene name: pam
Sequence domains: Aromatic amino acid lyase
Structure domains:

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 99.88Å b: 146.42Å c: 100.48Å
α: 90° β: 99.59° γ: 90°
R R work R free
0.18 0.178 0.207
Expression system: Escherichia coli