A theoretical study was performed to characterize noncovalent intermolecular interactions, especially hydrogen bond (HB), in the active site of enzyme human dehydroepiandrosterone sulphotransferase (SULT2A1/IDHEA) 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 Metl 6 in the active site of the SULT2A1/IDHEA. It was found that DHEA interacts with the other residues through electrostatic and Van der Waals interactions. (C) 2016 Elsevier B.V. All rights reserved.