Fig. 5 in Polyketide-derived macrobrevins from marine macroalga-associated Bacillus amyloliquefaciens as promising antibacterial agents against pathogens causing nosocomial infections

Fig. 5. (A) Molecular docking interfaces of 41-hydroxy-macrobrevin-31-acetate (compound 3) with S. aureus peptide deformylase (SaPDF). 3D docking analysis of the titled macrobrevin analogue (ligand) and S. aureus PDF crystal structure (PDB ID: 1LQW) were conformationally structured (Swiss-Pdb Viewer, SPDBV, version 4.1.0). The primary algorithm used by AutoDock for conformational searching was the Lamarckian Genetic Algorithm (LGA) showing four hydrogen bonds each (displayed as red and bluecoloured lines) in the binding site, whereas USCF Chimera (University of California, San Francisco, ver. 1.11.2) software reinforced the visualizations of the best molecular docking positions of the compound and target protein. The contact residues were shown and labeled by type and number in the background. Compound 3 exhibited least binding energy among the titled compounds. (B) Illustrative representation of 41-hydroxy-macrobrevin-31-acetate (compound 3) forming hydrogen bond interactions with the amino acyl residues in the active site of SaPDF. Compound (3) displayed maximum number of hydrogen bond interactions (GLN141 at 3.118 Å, LYS84 at 3.789 Å and 3.388 Å, and ARG143 at 3.483 Å). (C) Drug-likeness score obtained for the compound (3) with molsoft software. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)