Fig. 1
Subunit structure of Ch-CPN. Equatorial, intermediate, and apical domain are colored in green, cyan, and orange, respectively. The N- and C-termini are labeled as N and C, respectively. a Schematic representation of Cα tracing of Ch-CPN subunit. Four key residues connecting the domains are labeled. b Ribbon diagram of Ch-CPN subunit. The nucleotide-binding site and stem loop are indicated by a dotted circle and red ribbon, respectively. The key residues (I136, P198, A350, and G385) are marked by yellow, green, red, and purple circles, respectively. α-Helices and β-strands are numbered consecutively from the N-terminus to the C‐terminus. c Hydrophobic surface of the apical domain. The surfaces are colored based on the hydrophobicity of the side chains (from yellow for most hydrophobic, to lime for decreasing hydrophobicity). The crowded hydrophobic residues on the lid are labeled and presented as black sticks. d Residue conservation in the apical domain. Highly conserved residues are colored in purple. Amino acid sequences of the Group III CPNs which is used for residue conservation are described in Supplementary Fig. 2. The lid is indicated by a dotted circle
