› 1pfz

X-ray diffraction
1.85Å resolution

PROPLASMEPSIN II FROM PLASMODIUM FALCIPARUM

Released:
DOI: 10.2210/pdb1pfz/pdb
PDB entry 1pfz coloured by chain, front view.
PDB entry 1pfz coloured by chain, side view.
PDB entry 1pfz coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum.
Bernstein NK, Cherney MM, Loetscher H, Ridley RG, James MN
Nat Struct Biol 6 32-7 (1999)
PMID: 9886289

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:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-155535 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plasmepsin II Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 380 amino acids
Theoretical weight: 42.73 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: P46925 (Residues: 75-453; Coverage: 84%)
Gene name: PMII
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P21
Unit cell:
a: 52.007Å b: 133.223Å c: 114.234Å
α: 90° β: 98.45° γ: 90°
R-values:
R R work R free
0.214 0.214 0.237
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Biological roles of proteases in parasitic protozoa.
Klemba et al. (2002)
6 more

12 mentions without citation

Protonation and pK changes in protein-ligand binding.
Onufriev et al. (2013)
11 more