PDBe 1t6j

X-ray diffraction
2.1Å resolution

Crystal Structure of Phenylalanine Ammonia Lyase from Rhodosporidium toruloides

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine/tyrosine ammonia-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 714 amino acids
Theoretical weight: 77.66 KDa
Source organism: Rhodotorula toruloides
Expression system: Escherichia coli
UniProt:
  • Canonical: P11544 (Residues: 1-716; Coverage: 100%)
Gene name: PAL
Sequence domains: Aromatic amino acid lyase
Structure domains:

Ligands and Environments

1 bound ligand:

2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P3221
Unit cell:
a: 107.86Å b: 107.86Å c: 204.38Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.251 0.243 0.298
Expression system: Escherichia coli