Sulfotransferase 1A3 (SULT1A3) aids in the regulation of various endogenous and exogenous substrates in the body via sulfation. Specifically, this enzyme catalyzes the reaction that selectively sulfates dopamine and acetaminophen. In order to distinguish the selectivity of SULT1A3, the electronic interaction energies between the active site of this enzyme and a suite of molecules known to inhibit enzymes in the dopamine pathway have been calculated using M062X with the 6-311+G* basis set. The SULT1A3 active site was isolated from the crystal structure with dopamine bound (PBD ID:2A3R). Optimized structures for eleven ligands bound in the active site were obtained by M062X/6-31G with implicit solvation by water and relaxed amino acid side chains. At least one of the ligands currently studied would bind to SULT1A3 more strongly than dopamine and some previously studied ligands (D.J. Bigler et al. / Computational and Theoretical Chemistry 1051 (2015) 79–92).

DFT study of the binding of ligands in SULT1A3 active site

2019 Spring National Meeting

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