Fig. 3
hydrophobic pocket and the pocket factor. a A pocket is formed by E2 (green) subdomain D, E2 TM helix and E1 (blue) TM helix, depicted in ribbons, a 20 Å-long pocket factor was found to fill the pocket. The cryo-EM density of the pocket factor is colored in brown. The cryo-EM density of E1 and E2 are shown in gray with transparency value of 0.5. b The completely conserved (deep red) and highly conserved (pale red) amino acids composing the pocket are shown. c Hydrophobic phospholipid tail can be fitted well into the density of the pocket factor. The two completely conserved amino acids E2 P317 and E1 W409 forming hydrophobic interaction are shown. On the other side, E2 H314 forms hydrogen bonding with E1 S403. d It is hydrophobic inside the pocket. The surface of the protein is colored by surface potential
