› 1w6i

X-ray diffraction
2.7Å resolution

plasmepsin II-pepstatin A complex

Released:
DOI: 10.2210/pdb1w6i/pdb
PDB entry 1w6i coloured by chain, front view.
PDB entry 1w6i coloured by chain, side view.
PDB entry 1w6i coloured by chain, top view.
Source organisms:
Entry authors: Lindberg J, Johansson P-O, Rosenquist A, Kvarnstroem I, Vrang L, Samuelsson B, Unge T

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.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-155538 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Plasmepsin II Chains: A, C
Molecule details ›
Chains: A, C
Length: 331 amino acids
Theoretical weight: 37.12 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: P46925 (Residues: 123-453; Coverage: 73%)
Gene name: PMII
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
PEPSTATIN Chains: B, D
Molecule details ›
Chains: B, 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: MAX II BEAMLINE I711
Spacegroup: P3121
Unit cell:
a: 142.29Å b: 142.29Å c: 98.094Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.217 0.262
Expression systems:
  • Escherichia coli
  • Not provided

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