Fig. 2: Predicted binding mode of erythromycin.
From: Structural and functional insights into esterase-mediated macrolide resistance
Erythromycin modeled into the WT EreCClosed model showing catalytic amino acids and the interactions between the residues and the substrate. a Modeled structure of EreCClosed with erythromycin and water. The major lobe is displayed in light brown and the minor lobe in light pink. b A three-dimensional representation where protein residues are colored in teal, modeled alternate side-chain conformation of R261 in dark blue, erythromycin in green, and water molecule in red. The arrow indicating where the water molecule will attack erythromycin is shown in yellow. c Two-dimensional representation displaying the residues implied in the catalytic activity together with erythromycin. The color scheme of carbon atoms is the same as in (b). d Modification of (c) showing modeled alternate side-chain conformation of R261, and how it can interact with the transition state.
