X-ray diffraction
1.9Å resolution

Re-refinement of uncomplexed plasmepsin II from Plasmodium falciparum.


Function and Biology Details

Reaction catalysed:
Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO(2))-Ser-Phe-Pro-Thr.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Plasmepsin-2 Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 36.91 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
  • Canonical: P46925 (Residues: 125-453; Coverage: 73%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P2
Unit cell:
a: 52.659Å b: 39.567Å c: 90.532Å
α: 90° β: 105.54° γ: 90°
R R work R free
0.212 0.212 0.222
Expression system: Escherichia coli