Fig. 3: Interactions between CtAms1 and CtNbr1 FW domain.
From: Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1

a Overall view of the binding interfaces. The FW domain corresponds to the bottom right-hand molecule in Fig. 2a. CtAms1_3 is shown as an electrostatic potential surface. CtAms1_1 (green), CtAms1_4 (violet), and CtNbr1-FW (orange) are shown as ribbons. b Binding interface I between CtNbr1-FW and CtAms1_3. The interacting residues are labeled. Hydrogen bonds are denoted by black dashed lines. c Binding interface II between CtNbr1-FW and CtAms1_1. d Detailed interactions between the pocket of FW domain and the N-terminal peptide of CtAms1. e Electrostatic potential surface of the FW domain. The surface of the FW domain is colored in a blue-white-red gradient, with blue representing positive charge, red representing negative charge, and white representing neutral. The N-terminal peptide of CtAms1 is shown as sticks. f Space-filling representation of the pocket of FW domain bound to the N-terminal di-glycine of CtAms1. g Surface representation of the FW domain in opposite views. The residues within 4 Å of CtAms1 at the binding interface I and II are colored in brick red and cyan, respectively. Y739 was colored in light yellow. h Surface representation of the FW domain in opposite views. The residues with 92% and 70% conservation, as defined in Fig. 2d, are colored in orange and yellow, respectively.