Fig. 5: Active site and substrate-binding site views of CtdE–FAD-3 complex and its substrate-free structure. | Nature Communications

Fig. 5: Active site and substrate-binding site views of CtdE–FAD-3 complex and its substrate-free structure.

From: Structural basis of the stereoselective formation of the spirooxindole ring in the biosynthesis of citrinadins

Fig. 5: Active site and substrate-binding site views of CtdE–FAD-3 complex and its substrate-free structure.

a Overlay of the active site view of CtdE–FAD (residue carbons colored in white, FAD carbons colored in cyan) and CtdE–FAD-3 (residue carbons colored in light blue and FAD carbons colored in red) complexes. b Overlay of substrate-binding site view of CtdE–FAD (residues carbons colored in white) and CtdE–FAD-3 (residues carbons colored in light blue and carbons of compound 3 colored in red) complexes. c Analysis of the relative production rate of 3 with CtdE mutants. d Analysis of the relative production rate of 2 with CtdE mutants. Data represent the average of triplicate independent experiments (center values, mean; error bars, s.d.; n = 3).

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