PDBe 2oul

X-ray diffraction
2.2Å resolution

The Structure of Chagasin in Complex with a Cysteine Protease Clarifies the Binding Mode and Evolution of a New Inhibitor Family

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chagasin Chain: B
Molecule details ›
Chain: B
Length: 110 amino acids
Theoretical weight: 12.05 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q966X9 (Residues: 1-110; Coverage: 100%)
Gene name: cha
Sequence domains: Chagasin family peptidase inhibitor I42
Cysteine proteinase falcipain 2a Chain: A
Molecule details ›
Chain: A
Length: 241 amino acids
Theoretical weight: 27.19 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8I6U4 (Residues: 244-484; Coverage: 50%)
Gene names: PF11_0165, PF3D7_1115700
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P43212
Unit cell:
a: 94.236Å b: 94.236Å c: 119.764Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.232
Expression system: Escherichia coli