Triosephosphate isomerase from Fasciola hepatica: high-resolution crystal structure as a drug target

Kontellas, G.; Studholme, D.J.; van der Giezen, M.; Timson, D.J.; Littlechild, J.A.; Isupov, M.N.

doi:10.1107/S2053230X25006454

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 6
(a) Front view of the FhTPI dimer with the best docking pose of TCBZ (magenta) displayed. The dimer interface was used as the docking area. Active-site residues for each monomer are shown as red sticks. (b) Close-up view of the best docking pose showing TCBZ (magenta) docked close to the FhTPI dimer interface. Residues Lys50 and Asp51 (participating in the dimer interface) and residues within a radius of 4 Å from TCBZ are displayed. Active-site residues for each monomer are shown as red sticks. This image was produced with PyMOL (Schrödinger).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 81| Part 9| September 2025| Pages 381-387

https://doi.org/10.1107/S2053230X25006454

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