Bioassay’s Directed Isolation-Structure Elucidation and Molecular Docking of Triterpenes from Persea duthiei against Biologically Important Microbial Proteins

Figure 3

Putative binding interaction of compound 1 against bacterial S. aureus tyrosyl-tRNA synthetase. The THR75 (interacting with OH group of compound 1) and ASP177 (interacting with hydrogen atom of compound 1) residues of S. aureus tyrosyl-tRNA synthetase are hydrogen-bonded with OH group of compound 1, similar to its hydrogen bond formation with SB-284485 as previously reported. Similarly, HIS50 residue is also present in the active site of S. aureus tyrosyl-tRNA synthetase that interacts through hydrophobic bonding with the hydrophobic part of compound 1 in a similar fashion to that between SB-239629 and S. aureus tyrosyl-tRNA synthetase [30].