Figure 8

Figure 8

Molecular docking model to illustrate the key amino acid involved in Eno2-ePgk1 interaction. (A,B) Simulated model to illustrate how Eno2 (PDB ID: 5TD9) interacted with ePgk1 (PDB ID: 2ZGV) is presented in blue and orange, respectively. Drawing of partial enlargement of critical amino acid residues involved in Eno2-ePgk1 interaction was presented, including (A) wild-type Eno2 D419 and (B) mutant Eno2 D419S. The segment of the 345th to 360th amino acids of Pgk1, the segment of the 404th to 431st amino acid of Eno2, and the mutant Eno2 D419th were shown in Dodger blue, chocolate, and orange, respectively. (C,D) Drawing of partial enlargement of the surface polarity distribution of (C) Eno2 D419 and (D) Eno2 D419S. Dotted circles highlighted the D419th residue on Eno2. Lipophilicity was presented as low (hydrophilicity, in cyan) to high (hydrophobicity, in brown). Dotted zone indicates the 419th site. (E,F) Drawing of partial enlargement of the surface charge distribution of (E) Eno2 D419 and (F) Eno2 D419S. Chargeability from negative charge (in red) to positive charge (in blue). Dotted circles marked the 419th residue of Eno2.