› 5ltm

X-ray diffraction
2.41Å resolution

Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis (Y78F-C503S-C565S) bound to cinnamate

Released:
DOI: 10.2210/pdb5ltm/pdb
PDB 5ltm coloured by chain and viewed from the front.
PDB 5ltm coloured by chain and viewed from the side.
PDB 5ltm coloured by chain and viewed from the top.
Source organism: Anabaena
Primary publication:
Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes.
Weise NJ, Ahmed ST, Parmeggiani F, Galman JL, Dunstan MS, Charnock SJ, Leys D, Turner NJ
Sci Rep 7 13691 (2017)
PMID: 29057979

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine ammonia-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 537 amino acids
Theoretical weight: 58.74 KDa
Source organism: Anabaena
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q3M5Z3 (Residues: 25-563; Coverage: 95%)
Gene name: Ava_3988
Sequence domains: Aromatic amino acid lyase
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P4322
Unit cell:
a: 78.077Å b: 78.077Å c: 354.492Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.156 0.206
Expression system: Escherichia coli BL21

Quick links

Citations

6 citation in other articles

Fluorescent enzyme-coupled activity assay for phenylalanine ammonia-lyases.
Moisă et al. (2020)
5 more

3 mentions without citation

Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes.
Weise et al. (2017)
2 more