Fig. 3: Substrate-binding pocket and D-K loop in hSMPD2.
From: Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)
a Heatmap of the surface electrostatics of hSMPD2. Magnification of the Mg2+ and charged residues in the binding pocket of hSMPD2 (right). b Relative enzyme activity of wild type hSMPD2 and the indicated binding pocket-related mutants; mean ± SEM, n = 4 biological replicates. Source data are provided as a Source Data file. c Cylinder representation of hSMPD2 with the DK-loop regions were shown with side chain and superimposed into the cryo-EM density (left). The magnified view of the polar interactions between the DK loop and the neighboring residues (right). d The relative enzyme activity of WT and the DK loop related mutants in hSMPD2; mean ± SEM, n = 4 biological replicates. Source data are provided as a Source Data file.
