6SSZ
Structure of the Plasmodium falciparum falcipain 2 protease in complex with an (E)-chalcone inhibitor.
Summary for 6SSZ
| Entry DOI | 10.2210/pdb6ssz/pdb |
| Descriptor | Cysteine proteinase falcipain 2a, (~{E})-3-(1,3-benzodioxol-5-yl)-1-(3-nitrophenyl)prop-2-en-1-one (2 entities in total) |
| Functional Keywords | inhibitor, complex, malaria, haemoglobin, proteolysis, hydrolase |
| Biological source | Plasmodium falciparum |
| Total number of polymer chains | 2 |
| Total formula weight | 54953.84 |
| Authors | Machin, J.,Kantsadi, A.,Vakonakis, I. (deposition date: 2019-09-09, release date: 2019-12-04, Last modification date: 2024-11-20) |
| Primary citation | Machin, J.M.,Kantsadi, A.L.,Vakonakis, I. The complex of Plasmodium falciparum falcipain-2 protease with an (E)-chalcone-based inhibitor highlights a novel, small, molecule-binding site. Malar.J., 18:388-388, 2019 Cited by PubMed Abstract: Malaria kills over 400,000 people each year and nearly half the world's population live in at-risk areas. Progress against malaria has recently stalled, highlighting the need for developing novel therapeutics. The parasite haemoglobin degradation pathway, active in the blood stage of the disease where malaria symptoms and lethality manifest, is a well-established drug target. A key enzyme in this pathway is the papain-type protease falcipain-2. PubMed: 31791339DOI: 10.1186/s12936-019-3043-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.45 Å) |
Structure validation
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