Fig. 4: MD simulations of the sphingomyelin binding within hSMPD2.
From: Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)
a MD simulations reveal the binding pose of sphingomyelin within the binding pocket. The magnesium ion is shown as a green sphere. b A representative MD pose reveals that the side chain of K116 could form a salt bridge with the phosphate group of the binding sphingomyelin. c Multiple unbiased MD simulations revealed the lysine-phosphate salt bridge would be well maintained during the production run phase. d Relative enzyme activity of wild type hSMPD2 and the indicated sphingomyelin-binding-pocket-related mutants; mean ± SEM, n = 4 biological replicates. Source data are provided as a Source Data file.
