› 2fu0

X-ray diffraction
1.8Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184668 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PPIase cyclophilin-type domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 18.19 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8I402 (Residues: 589-747; Coverage: 21%)
Gene name: PF3D7_0510200
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 FR-E
Spacegroup: P21
Unit cell:
a: 32.164Å b: 56.301Å c: 39.712Å
α: 90° β: 107.89° γ: 90°
R-values:
R R work R free
0.174 0.171 0.221
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

2 mentions without citation

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