X-ray diffraction
2.7Å resolution

Crystal Structure of Mutant Cyclophilin (R147A) from Leishmania donovani

Source organism: Leishmania donovani
Entry authors: Venugopal V, Sen B, Datta AK, Banerjee R

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 19 KDa
Source organism: Leishmania donovani
Expression system: Escherichia coli
  • Canonical: Q9U9R3 (Residues: 22-187; Coverage: 100%)
Gene name: CYP
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P65
Unit cell:
a: 74.973Å b: 74.973Å c: 61.323Å
α: 90° β: 90° γ: 120°
R R work R free
0.158 0.158 0.226
Expression system: Escherichia coli