Fig. 4: Contribution of FAD moieties to dCRY folding. | Nature Communications

Fig. 4: Contribution of FAD moieties to dCRY folding.

From: The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments

Fig. 4

a Contact map between FAD moieties and amino acid residues in dCRY. Interactions include hydrogen bonding (gray), hydrophobic effect (purple), metal coordination (dark teal) and cation-pi interactions (ochre). b Bar plot representing the percentage of dCRY in the folded state in the presence of different cofactors. c Bar plot of percentage of dCRY intermediate states bound to adenosine, AMP, ADP and ATP. d Bar plots of percentage of dCRY in an unbound intermediate, bound intermediate or folded state in the presence of ADP or ATP, with and without Mg2+. Source data for panels b–d are available as a Source Data file.

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