› 2cmt

X-ray diffraction
1.5Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173250 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase E Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 19.22 KDa
Source organism: Schistosoma mansoni
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q26548 (Residues: 102-273; Coverage: 63%)
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

1 bound ligand:
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 39.654Å b: 59.213Å c: 61.888Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.205
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Schistosoma genomics: new perspectives on schistosome biology and host-parasite interaction.
Han et al. (2009)
2 more

3 mentions without citation

Redox-assisted protein folding systems in eukaryotic parasites.
Haque et al. (2012)
2 more