› 2igy

X-ray diffraction
2.6Å resolution

Achiral, Cheap and Potent Inhibitors of Plasmepsins II

Released:
DOI: 10.2210/pdb2igy/pdb
PDB entry 2igy coloured by chain, front view.
PDB entry 2igy coloured by chain, side view.
PDB entry 2igy coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Achiral, cheap, and potent inhibitors of Plasmepsins I, II, and IV.
Boss C, Corminboeuf O, Grisostomi C, Meyer S, Jones AF, Prade L, Binkert C, Fischli W, Weller T, Bur D
ChemMedChem 1 1341-5 (2006)
PMID: 17091526

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155535 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plasmepsin II Chains: A, B
Molecule details ›
Chains: A, B
Length: 329 amino acids
Theoretical weight: 36.95 KDa
Source organism: Plasmodium falciparum
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:
Ligand A2T 2 x A2T
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3212
Unit cell:
a: 161.099Å b: 161.099Å c: 73.932Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.214 0.211 0.264

Quick links

Citations

3 review citations

Molecular recognition in chemical and biological systems.
Persch et al. (2015)
2 more

8 mentions without citation

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