Extended Data Fig. 5: Ligand densities in the N-pocket, C-pocket, inter-pocket, and on the back-surface around the α-syn fibril.
From: Structural mechanism for specific binding of chemical compounds to amyloid fibrils
a, Structure model of the α-syn fibril with all residues and pockets labeled. b, For each ligand-binding pocket/surface around the α-syn fibril, cryo-EM densities and structures are shown and colored in gray. For each ligand, their densities are shown and colored in line with the ligand color. The protein density is restricted to areas within a 2-Å radius of the α-syn model, and combined with the ligand densities displayed with the same threshold: CCA, 0.0096; CR, 0.008; EB, 0.013; ThT, 0.0098; BF227a, 0.0045; PiB, 0.0085; C05-03, 0.0045; SIL5, 0.0069; pFTAA, 0.0233. Chemical structures of the ligands are provided under the ligand names.
