PDBe 3bpm

X-ray diffraction
2.5Å resolution

Crystal Structure of Falcipain-3 with Its inhibitor, Leupeptin


Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Leupeptin Chains: C, D
Molecule details ›
Chains: C, D
Length: 4 amino acids
Theoretical weight: 430 Da
Source organism: Streptomyces roseus
Expression system: Not provided
Cysteine protease falcipain-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 243 amino acids
Theoretical weight: 27.38 KDa
Source organism: Plasmodium falciparum
  • Canonical: Q9NAW4 (Residues: 250-492; Coverage: 49%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: R32
Unit cell:
a: 154.57Å b: 154.57Å c: 129.011Å
α: 90° β: 90° γ: 120°
R R work R free
0.191 0.19 0.224
Expression system: Not provided