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structure of plasmepsin II from Plasmodium Falciparum complexed with inhibitor DR718A

Source organism: Plasmodium falciparum
Biochemical function: aspartic-type endopeptidase activity
Biological process: proteolysis
Cellular component: not assigned

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EC 3.4.23.39: Plasmepsin II

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.
Alternative Name(s):
  • Aspartic hemoglobinase II
  • PFAPD
  • PfAPD

GO terms

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF00026
Domain description: Eukaryotic aspartyl protease
Occurring in:
  1. Plasmepsin II
The deposited structure of PDB entry 4z22 contains 2 copies of Pfam domain PF00026 (Eukaryotic aspartyl protease) in Plasmepsin II. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR001461
Domain description: Aspartic peptidase A1
Occurring in:
  1. Plasmepsin II
IPR021109
Domain description: Aspartic peptidase domain superfamily
Occurring in:
  1. Plasmepsin II
IPR001969
Domain description: Aspartic peptidase, active site
Occurring in:
  1. Plasmepsin II
IPR033121
Domain description: Peptidase family A1 domain
Occurring in:
  1. Plasmepsin II
IPR034164
Domain description: Pepsin-like domain
Occurring in:
  1. Plasmepsin II

Structure domain

CATH CATH domain
2.40.70.10
Class: Mainly Beta
Architecture: Beta Barrel
Topology: Cathepsin D, subunit A; domain 1
Homology: Acid Proteases
Occurring in:
  1. Plasmepsin II
The deposited structure of PDB entry 4z22 contains 4 copies of CATH domain 2.40.70.10 (Cathepsin D, subunit A; domain 1) in Plasmepsin II. Showing 2 copies in chain A.

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