1qyj

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

HISTOASPARTIC PROTEINASE FROM PLASMODIUM FALCIPARUMHISTOASPARTIC PROTEINASE FROM PLASMODIUM FALCIPARUM

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed The primary structure of the so-called histoaspartic protease from Plasmodium falciparum has a very high percentage of identity and homology with the pepsin-like enzyme plasmepsin II. A homology modeling approach was used to calculate the three-dimensional structure of the enzyme. Molecular dynamics (MD) simulations were applied to find those structural properties of the histoaspartic protease that had a tendency to remain stable during all runs. The results have shown that hydrogen-bonded residues Ser37-His34-Asp214 are arranged without any strain, in a manner that resembles the active site of a serine protease, while Ser38 and Asn39 take up positions appropriate to formation of an oxyanion hole. Although there are several important differences between the enzyme and plasmepsin II, all of the structural features associated with a typical pepsin-like aspartic protease are present in the final model of the histoaspartic protease. A possibility that this enzyme may function as a serine protease is discussed. Is histoaspartic protease a serine protease with a pepsin-like fold?,Andreeva N, Bogdanovich P, Kashparov I, Popov M, Stengach M Proteins. 2004 May 15;55(3):705-10. PMID:15103632 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1qyj Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image