The mouse cytosolic sulfotransferase, mSULT1D1, catalyzes the sulfonation of a wide range of phenolic molecules including p-nitrophenol (pNP), alpha-naphthol (alpha NT), serotonin, as well as dopamine and its metabolites. To gain insight into the Structural basis for its broad range Substrate specificity, we solved two distinct ternary crystal structures of mSULT1D1, complexed with 3'-phosphoadenosine-5'-phosphate (PAP) plus pNP OF PAP plus alpha NT. The structures revealed that the mSULT1D1 contains an L-shaped accepter-binding site which comprises 20 amino acid residues and four conserved water molecules. The shape of the accepter-binding site can be adjusted by conformational changes of two residues, Ile148 and Glu247, upon binding with respective substrates. (C) 2008 Elsevier Inc. All rights reserved.