Reconstruction of the spatial structure of plant phosphatases types 1 and 2A in complexes with okadaic acid

Homology modeling based on the known spatial structures of Homo sapiens protein phosphatases types 1 and 2A was implemented. The spatial structures of human protein phosphatases and their plant homologs from Arabidopsis thaliana were predicted. The quality of the models was confirmed by the root mean square deviations of the atoms and conformational analysis results. The sites of okadaic acid bindings in the molecules of plant protein phosphatases (types 1 and 2A) were verified by the data of comparative analyses and molecular dynamics.