› 4v2r

X-ray diffraction
2.2Å resolution

Ironing out their differences: Dissecting the structural determinants of a phenylalanine aminomutase and ammonia lyase

Released:
DOI: 10.2210/pdb4v2r/pdb
PDB entry 4v2r coloured by chain, front view.
PDB entry 4v2r coloured by chain, side view.
PDB entry 4v2r coloured by chain, top view.
Source organism: Taxus chinensis
Primary publication:
Ironing out their differences: dissecting the structural determinants of a phenylalanine aminomutase and ammonia lyase.
Heberling MM, Masman MF, Bartsch S, Wybenga GG, Dijkstra BW, Marrink SJ, Janssen DB
ACS Chem Biol 10 989-97 (2015)
PMID: 25494407

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179344 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine aminomutase (L-beta-phenylalanine forming) Chains: A, B
Molecule details ›
Chains: A, B
Length: 705 amino acids
Theoretical weight: 77.5 KDa
Source organism: Taxus chinensis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q68G84 (Residues: 1-687; Coverage: 100%)
Gene name: pam
Sequence domains: Aromatic amino acid lyase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MDO 2 x MDO

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 181.485Å b: 76.486Å c: 120.419Å
α: 90° β: 120.02° γ: 90°
R-values:
R R work R free
0.213 0.212 0.247
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Biochemical and Structural Analysis of Substrate Specificity of a Phenylalanine Ammonia-Lyase.
Jun et al. (2018)
8 more