3juo

X-ray diffraction
2.2Å resolution

Crystal Structure of PhzA/B from Burkholderia cepacia R18194 in complex with (R)-5-bromo-2-(piperidin-3-ylamino)benzoic acid

Released:
Source organism: Burkholderia lata
Primary publication:
The active site of an enzyme can host both enantiomers of a racemic ligand simultaneously.
Angew. Chem. Int. Ed. Engl. 48 9084-7 (2009)
PMID: 19876985

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenazine biosynthesis protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 185 amino acids
Theoretical weight: 21.53 KDa
Source organism: Burkholderia lata
Expression system: Escherichia coli
UniProt:
  • Canonical: Q396C9 (Residues: 1-165; Coverage: 100%)
Gene name: Bcep18194_B1568
Sequence domains: Phenazine biosynthesis protein A/B
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3221
Unit cell:
a: 64.6Å b: 64.6Å c: 160.89Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.18 0.223
Expression system: Escherichia coli