Noncovalent intermolecular interactions between dehydroepiandrosterone and the active site of human dehydroepiandrosterone sulphotransferase: A density functional theory based treatment

• DOI: 10.1016/j.cplett.2016.01.064
• Publication Date: 2016-02-24T16:48:16Z
• Authors: Elahe Astani; Emran Heshmati; Chun-Jung Chen; Nasser L. Hadipour; Setareh Shekarsaraei
• Keywords: Non-covalent interactions

Abstract A theoretical study was performed to characterize noncovalent intermolecular interactions, especially hydrogen bond (HB), in the active site of enzyme human dehydroepiandrosterone sulphotransferase (SULT2A1/DHEA) using the local (M06-L) and hybrid (M06, M06-2X) meta-GGA functionals of density functional theory (DFT). Results revealed that DHEA is able to form HBs with residues His99, Tyr231, Met137 and Met16 in the active site of the SULT2A1/DHEA. It was found that DHEA interacts with the other residues through electrostatic and Van der Waals interactions.