7QON
Monoclinic triose phosphate isomerase from Fasciola hepatica.
This is a non-PDB format compatible entry.
Summary for 7QON
| Entry DOI | 10.2210/pdb7qon/pdb |
| Descriptor | Triosephosphate isomerase, SODIUM ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | fasciolysis, isomerase |
| Biological source | Fasciola hepatica (liver fluke) |
| Total number of polymer chains | 4 |
| Total formula weight | 112769.84 |
| Authors | Kontellas, G.,Isupov, M.N.,Littlechild, J.A. (deposition date: 2021-12-24, release date: 2023-01-18, Last modification date: 2025-10-22) |
| Primary citation | Kontellas, G.,Studholme, D.J.,van der Giezen, M.,Timson, D.J.,Littlechild, J.A.,Isupov, M.N. Triosephosphate isomerase from Fasciola hepatica: high-resolution crystal structure as a drug target. Acta Crystallogr.,Sect.F, 81:381-387, 2025 Cited by PubMed Abstract: The trematode liver fluke Fasciola hepatica causes the neglected tropical disease fascioliasis in humans and is associated with significant losses in agricultural industry due to reduced animal productivity. Triosephosphate isomerase (TPI) is a glycolytic enzyme that has been researched as a drug target for various parasites, including F. hepatica. The high-resolution crystal structure of F. hepatica TPI (FhTPI) has been solved at 1.51 Å resolution in its monoclinic form. The structure has been used to perform molecular-docking studies with the most successful fasciolocide triclabendazole (TCBZ), which has recently been suggested to target FhTPI. Two FhTPI residues, Lys50 and Asp51, are located at the dimer interface and are found in close proximity to the docked TCBZ. These residues are not conserved in mammalian hosts. PubMed: 40832834DOI: 10.1107/S2053230X25006454 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.51 Å) |
Structure validation
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