Extended Data Fig. 5: Detailed environment of the FAD binding cavity in the BIC2-CRY2N complex.

a, Sequence conservation analysis and close up view of the FAD binding cavity in BIC2-CRY2N. The FAD binding cavity is mainly formed by the CRY2N α9, α10, α12, α15, α16, α17 helices, shown in the black box at right. Sequence conservation scores displayed in different colors on the surface of CRY2 were generated by the CONSURF program. The FAD and AMP molecules are presented as green and pink ball-and-stick models. The magnesium cation is colored in magenta. b, Interface between BIC2 helix α1 and the phosphate binding loop between the α9 and α10 helices of CRY2N. Yellow dashed lines denote hydrogen bonds. c, FAD and AMP molecules in the BIC2-CRY2N complex are presented as ball-and-stick models. d, FAD displays a U-shaped conformation. The electron density (blue) of FAD is contoured at 1σ. e, Schematic representation of the contacts between CRY2 and FAD. f, Stereo representation of the electron density map of AMP bound to BIC2-CRY2N complex. The 2Fo-Fc electron density (1σ level) of AMP is shown in blue. g, The binding site of AMP. AMP is recognized by CRY2 residues N356, R357, Y399, and D406. Hydrogen bonds are shown as yellow dashed lines.