1m43

X-ray diffraction
2.4Å resolution

Crystal structure of PMII in complex with pepstatin a to 2.4 A

Released:
Entry authors: Asojo OA, Silva AM, Gulnik S

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:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Plasmepsin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 331 amino acids
Theoretical weight: 37.08 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: P46925 (Residues: 123-453; Coverage: 73%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Pepstatin Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 686 Da
Source organism: Streptomyces argenteolus subsp. toyonakensis
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9A
Spacegroup: P3121
Unit cell:
a: 142.235Å b: 142.235Å c: 97.892Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.197 0.245
Expression systems:
  • Escherichia coli
  • Not provided