› 1z81

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181903 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 25.97 KDa
Source organism: Plasmodium yoelii yoelii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7RSH5 (Residues: 1-210; Coverage: 100%)
Gene name: PY00382
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: APS BEAMLINE 17-ID
Spacegroup: P43212
Unit cell:
a: 64.23Å b: 64.23Å c: 156.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.266 0.257 0.285
Expression system: Escherichia coli

Quick links

Citations

33 review citations

Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.
Hall et al. (2011)
32 more

3 mentions without citation

Structural insights into Plasmodium PPIases.
Rajan et al. (2022)
2 more