Fig. 2
The surfaces of the FAT10 UBDs are distinct from Ub and each other. a Structure-based sequence alignment of the human FAT10 domains with Ub. Residues are color coded by sequence identity from white (0%) to dark blue (100%). Secondary structure elements are labeled and boxed. The residues corresponding to the hydrophobic patch in Ub are marked with asterisks. b Close-up on the residues equivalent to the hydrophobic patch in Ub showing the N-domain (top), the C-domain (center), and Ub (bottom). c Electrostatic surface potentials of the FAT10 N- (top) and C-domains (center) and Ub (bottom). Negatively charged areas are colored in red, while positively charged regions are in blue and neutral residues in white. The position of the hydrophobic patch residues in Ub and equivalent positions in the FAT10 domains are labeled. The boxes outline the close-up regions depicted in b. d Surface plots of the FAT10 N- (red; top) and C-domains (teal; center) colored by conservation of residues in mammalian FAT10 proteins (Supplementary Fig. 4). Highly conserved residues are labeled. The surface of Ub is color coded in green by occurrence of residues at the interfaces of Ub–protein complexes (bottom). All structure and surface representations are in the same orientation as in Fig. 1d–f
