Fig. 3
From: Chemical logic of MraY inhibition by antibacterial nucleoside natural products

Capuramycin forms a unique interaction with the caprolactam site on MraYAA. a The binding pockets occupied by capuramycin (yellow) on the cytoplasmic face of MraYAA include the uridine (red), uridine-adjacent (lime green), and caprolactam (pink) sites. b A zoomed-in view of the capuramycin binding site in the same orientation as shown in a. Residues forming interactions with capuramycin are labeled and color-coded according to the binding pocket to which they belong. Hydrogen bonds are represented by dashed lines. c A view of the capuramycin binding site rotated 60° relative to the orientation in a to highlight the caprolactam binding site. The surface of MraYAA is shown in transparent gray with residues forming the shallow caprolactam binding pocket (pink dashes lines) labeled. TMs (numbers) and Loops (letters) are labeled throughout. The side chains of residues K70 and K121 are disordered in the MraYAA-capuramycin complex structure