Extended Data Fig. 4: The ligand-enzyme interactions in the NADPH binding pocket of EasCCf.
From: Chanoclavine synthase operates by an NADPH-independent superoxide mechanism
a, Detailed interaction between PCC and EasCCf characterized by LigandPlot. PCC shown in blue sticks and coloured by atom type. Polar and hydrophobic interactions were mapped with the LigPlot program and indicated with dashed lines or a starburst symbol. b, The mutational results of key residues of EasCCf. The enzyme activity of each sample is calculated as a percentage of the wild type enzyme (WT). The individual (n = 3) and average values along with error bars (s.d.) of each group in one representative experiment among three independent experiments are shown. c, ITC measurement of PCC binding to corresponding EasCCf mutants. EasCCf-WT and F185A was observed to interact with PCC. The KD was determined to 6.21 ± 0.19 µM and 39.5 ± 6.37 µM, respectively. Heat changes measured as a function of time at 25 °C are shown. (Lower) Normalized heat changes (filled square) and the best-fit curve (solid line) are shown.
