1qnh

X-ray diffraction
2.1Å resolution

Plasmodium falciparum Cyclophilin (double mutant) complexed with Cyclosporin A

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 170 amino acids
Theoretical weight: 18.88 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q25756 (Residues: 2-171; Coverage: 99%)
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
CYCLOSPORIN A Chains: C, D
Molecule details ›
Chains: C, D
Length: 11 amino acids
Theoretical weight: 1.22 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided

Ligands and Environments

No bound ligands

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21212
Unit cell:
a: 92.11Å b: 115.12Å c: 39.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 0.21
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided