PDBe 3fns

X-ray diffraction
2.5Å resolution

Crystal structure of histo-aspartic protease (HAP) from Plasmodium Falciparum

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plasmepsin III Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 37.44 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IM15 (Residues: 120-451; Coverage: 74%)
Gene names: PF14_0078, PF3D7_1408100
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P41212
Unit cell:
a: 89.8Å b: 89.8Å c: 198.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.225 0.274
Expression system: Escherichia coli