› 1w27

X-ray diffraction
1.7Å resolution

Phenylalanine ammonia-lyase (PAL) from Petroselinum crispum

Released:
DOI: 10.2210/pdb1w27/pdb
PDB entry 1w27 coloured by chain, front view.
PDB entry 1w27 coloured by chain, side view.
PDB entry 1w27 coloured by chain, top view.
Source organism: Petroselinum crispum
Primary publication:
Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase.
Ritter H, Schulz GE
Plant Cell 16 3426-36 (2004)
PMID: 15548745

Function and Biology Details

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

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: 714 amino acids
Theoretical weight: 77.88 KDa
Source organism: Petroselinum crispum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P24481 (Residues: 1-716; Coverage: 100%)
Gene name: PAL1
Sequence domains: Aromatic amino acid lyase
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: C2221
Unit cell:
a: 119.96Å b: 160.81Å c: 141.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.199
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Phenylpropanoid biosynthesis.
Vogt T. (2010)
12 more

16 mentions without citation

Structure and function of enzymes involved in the biosynthesis of phenylpropanoids.
Ferrer et al. (2008)
15 more