Fig. 3: Structural comparison of WT RBD-hACE2 and each SARS-CoV-2 variants RBD-hACE2. | Nature Communications

Fig. 3: Structural comparison of WT RBD-hACE2 and each SARS-CoV-2 variants RBD-hACE2.

From: Molecular insights into receptor binding of recent emerging SARS-CoV-2 variants

Fig. 3

a–e The WT RBD-hACE2 structure (PDB: 6LZG) is shown in the center. Superimposition of WT RBD-hACE2 and each variant RBD-hACE2 (including Beta RBD-hACE2 (a), Gamma RBD-hACE2 (b), Alpha RBD-hACE2 (c), Mink-F486L RBD-hACE2 (d), Mink-Y453F RBD-hACE2 (e)) are shown in each surrounding panel. In each structure the hACE2 is colored in light pink. SARS-CoV-2 WT RBD, Beta RBD, Gamma RBD, Alpha RBD, Mink-F486L RBD, and Mink-Y453F RBD are colored in gray, cyan, orange, yellow, green, and magenta, respectively. The key contact residues are shown as stick structures and labeled appropriately. The cation-π interaction, π-π stacking interaction, salt bridge, and hydrogen bonds are colored in magenta, blue, orange, and yellow, respectively. Hydrogen bond interactions were analyzed at a cutoff of 3.5 Å. f The detailed hydrogen bonds between the Mink-Y453F RBD and hACE2 are shown.

Back to article page