1lee

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF PLASMEPSIN FROM P. FALCIPARUM IN COMPLEX WITH INHIBITOR RS367

Released:

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

Assemblies composition:
monomeric (preferred)
homo dimer
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plasmepsin-2 Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 37.08 KDa
Source organism: Plasmodium falciparum
UniProt:
  • Canonical: P46925 (Residues: 123-453; Coverage: 73%)
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: NSLS BEAMLINE X9B
Spacegroup: I222
Unit cell:
a: 75.89Å b: 84.83Å c: 123.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.236 0.286