› 4c5r

X-ray diffraction
2.14Å resolution

Structural Investigations into the Stereochemistry and Activity of a Phenylalanine-2,3-Aminomutase from Taxus chinensis

Released:
DOI: 10.2210/pdb4c5r/pdb
PDB entry 4c5r coloured by chain, front view.
PDB entry 4c5r coloured by chain, side view.
PDB entry 4c5r coloured by chain, top view.
Source organism: Taxus chinensis
Primary publication:
Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from Taxus chinensis.
Wybenga GG, Szymanski W, Wu B, Feringa BL, Janssen DB, Dijkstra BW
Biochemistry 53 3187-98 (2014)
PMID: 24786474

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 705 amino acids
Theoretical weight: 77.55 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

2 bound ligands:
Ligand BQ7 4 x BQ7
Ligand GOL 2 x GOL
1 modified residue:
Ligand MDO 4 x MDO

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 99.395Å b: 145.477Å c: 99.564Å
α: 90° β: 99.54° γ: 90°
R-values:
R R work R free
0.174 0.172 0.21
Expression system: Escherichia coli

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Citations

1 review citation

Dehydroamino acids: chemical multi-tools for late-stage diversification.
Bogart et al. (2019)
6 other articles