Extended Data Fig. 9: Structural comparison between LPP1-C3M and G6PC1.
From: Structural basis for the catalytic mechanism of human lipid phosphate phosphatases
a, Two perpendicular views illustrate the structural superimposition of LPP1-C3M and G6PC1 (PDB: 9J7U). Inset: Zoomed-in views highlighting key essential elements within the catalytic cavities. b, Separate views displaying the electrostatic surface potentials of LPP1-C3M and G6PC1. The middle section presents zoomed-in views of the catalytic cavities of LPP1-C3M and G6PC1. The clashes between G6P and the LPP1-C3M cavity are indicated. The G6PC1 cavity lacks sufficient space to accommodate the hydrophobic tails of the LPP1 substrates. c, Functional assays indicate that LPP1 exhibits low activity in dephosphorylation of glucose 6-phosphate (G6P). Data are presented as the means ± s.d. of three independent experiments, each with two technical repeats (n=6).
