Fig. 6: SBTs for transglycosylation. | Nature Communications

Fig. 6: SBTs for transglycosylation.

From: Elucidation of the noncovalent interactions driving enzyme activity guides branching enzyme engineering for α-glucan modification

Fig. 6: SBTs for transglycosylation.

a Docking results of the acceptor polysaccharide chains (cyan and white) for transglycosylation. The carbon atoms of the donor polysaccharide chain in the active-site cleft are colored in green. b Hydrogen-bonding interactions of the acceptor polysaccharide chain (pose I) with the adjacent twelve residues. The polysaccharide chain and the adjacent residues are shown in a licorice representation, and their carbon atoms are colored in cyan and orange, respectively. c Distance (Å) separating the COM of the polysaccharide chain and the catalytic triad with the time course in each assembly. A distance greater than 17 Å means that the polysaccharide chain has separated from the active-site cleft. d and e Interactions of the polysaccharide chain with the protein and the adjacent residues, respectively. Source data for c–e are provided as a Source Data file.

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