Fig. 3

C2CD3 (C2 calcium-dependent domain containing 3) protein has six canonical PKC-C2 domains and a C2CD3N–C2 domain at the N-terminus [25]. The graph showed the conserved amino acid residues at the 577 and 907 positions on C2CD3 protein (A). The iterative threading assembly refinement (I-TASSER) server was used to predict the three-dimensional structure of wild type (B and D) and mutant (C and E) C2CD3 protein. The yellow dashed line indicates the hydrogen bond. (C) The H577 residue is predicted to form a new hydrogen bond with V623 residue, which slightly changed the β-sheet structure. (E) The C907 residue is predicted to cause hydrogen bond loss with H904 and F910 and form a new hydrogen bond with the S909 residue, affecting the proper protein folding in the α‐helix