› 6rgs

X-ray diffraction
2.42Å resolution

Crystal Structure of Phenylalanine Ammonia Lyase (PAL) from Petroselinum crispum bound to cinnamate

Released:
DOI: 10.2210/pdb6rgs/pdb
PDB entry 6rgs coloured by chain, front view.
PDB entry 6rgs coloured by chain, side view.
PDB entry 6rgs coloured by chain, top view.
Source organism: Petroselinum crispum
Primary publication:
Mapping the Hydrophobic Substrate Binding Site of Phenylalanine Ammonia Lyase from Petroselinum crispum
Nagy EZA, Tork SD, Lang PA, Filip A, Irimie FD, Poppe L, Tosa MI, Schofield CJ, Brem J, Paizs C, Bencze LC
ACS Catalysis (2019)

Function and Biology Details

Reaction catalysed: 
L-phenylalanine = trans-cinnamate + ammonia
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150239 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine ammonia-lyase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 740 amino acids
Theoretical weight: 80.99 KDa
Source organism: Petroselinum crispum
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P24481 (Residues: 1-715; Coverage: 100%)
Gene name: PAL1
Sequence domains: Aromatic amino acid lyase

Ligands and Environments

1 bound ligand:
Ligand K3Z 1 x K3Z
1 modified residue:
Ligand MDO 2 x MDO

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 119.91Å b: 159.82Å c: 142.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.21 0.238
Expression system: Escherichia coli BL21

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