› 1qs8

X-ray diffraction
2.5Å resolution

Crystal structure of the P. vivax aspartic proteinase plasmepsin complexed with the inhibitor pepstatin A

Released:
DOI: 10.2210/pdb1qs8/pdb
PDB entry 1qs8 coloured by chain, front view.
PDB entry 1qs8 coloured by chain, side view.
PDB entry 1qs8 coloured by chain, top view.
Source organisms:
Primary publication:
Structural insights into the activation of P. vivax plasmepsin.
Bernstein NK, Cherney MM, Yowell CA, Dame JB, James MN
J Mol Biol 329 505-24 (2003)
PMID: 12767832

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
hetero octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-130226 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase A1 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 329 amino acids
Theoretical weight: 37.16 KDa
Source organism: Plasmodium vivax
Expression system: Bacteria
UniProt:
  • Canonical: O60989 (Residues: 122-450; Coverage: 73%)
Gene names: PVC01_130047600, PVT01_130045800, PVW1_130047400
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
PEPSTATIN A 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

1 bound ligand:
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P41212
Unit cell:
a: 145.015Å b: 145.015Å c: 71.072Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.25
Expression systems:
  • Bacteria
  • Not provided

Quick links

Citations

3 review citations

Plasmepsins as potential targets for new antimalarial therapy.
Ersmark et al. (2006)
2 more

5 mentions without citation

Structural studies of vacuolar plasmepsins.
Bhaumik et al. (2012)
4 more