4cku

X-ray diffraction
1.85Å resolution

Three dimensional structure of plasmepsin II in complex with hydroxyethylamine-based inhibitor

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

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155544 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plasmepsin II Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 329 amino acids
Theoretical weight: 36.91 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P46925 (Residues: 125-453; Coverage: 73%)
Gene name: PMII
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: MAX II BEAMLINE I911-3
Spacegroup: C2
Unit cell:
a: 201.95Å b: 115.25Å c: 93.17Å
α: 90° β: 110.75° γ: 90°
R-values:
R R work R free
0.16 0.158 0.209
Expression system: Escherichia coli BL21(DE3)