Fig. 6: The docking model of AlpH in complex with the product 9.
From: O-methyltransferase-like enzyme catalyzed diazo installation in polyketide biosynthesis

a Combination of a surface representation and the stick-ball model showing the overall docking model of a monomeric AlpH in complex with the product 9. The fitted product 9 is shown in stick model (orange) and is embedded in the pocket between the N-terminal dimerization domain and the C-terminal catalytic domain. b Surface representation showing the overall docking model of a monomeric AlpH in complex with the product 9 with the same orientation as in panel A. Specifically, the amino acid residues were colored as yellow (hydrophobic amino acid), blue (positively charged amino acid), red (negatively charged amino acid), and gray (uncharged polar amino acid). c The combined ribbon diagram and the stick-ball model showing the detailed interactions between AlpH and the fitted product 9. The related hydrogen bonds and salt bridges involved in the binding are shown as dotted lines. d A structural modeling analysis of the product 9 and SAH in binding to AlpH revealing that AlpH is unable to simultaneously interact with the product 9 and SAH. e Relative activities of AlpH mutants. The columns represent the average values of the products (the highest mean value was set 100%); bars indicate ± SD (standard deviation) of n = 3 independent replicates. Source data are provided as a Source Data file.