PDBe 4dz2

X-ray diffraction
2Å resolution

Crystal structure of a Peptidyl-prolyl cis-trans isomerase with surface mutation R92G from Burkholderia pseudomallei complexed with FK506


Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0). 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Peptidyl-prolyl cis-trans isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 113 amino acids
Theoretical weight: 11.8 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q3JK38 (Residues: 2-113; Coverage: 99%)
Gene name: BURPS1710b_A0907
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 106.44Å b: 49.05Å c: 66.64Å
α: 90° β: 123.05° γ: 90°
R R work R free
0.22 0.219 0.247
Expression system: Escherichia coli BL21(DE3)