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Fig. 5 | BMC Chemistry

Fig. 5

From: Design, computational studies, synthesis and in vitro antimicrobial evaluation of benzimidazole based thio-oxadiazole and thio-thiadiazole analogues

Fig. 5

Multiple sequence alignment [33] of PheRS α subunit amino acid sequences from Th. thermophilus (Q5SGX2), P. aeruginosa (Q9I0A3), K. pneumoniae (A6TAI3), E. coli (P08312), S. aureus (P68849) and E. faecalis (Q836J6). The purple box shows the conserved phenylalanine residue responsible for hydrophobic stabilisation of the adenine moiety in Phe-AMP. The green boxes show the conserved arginine residues responsible for the hydrophilic interactions that stabilise the AMP moiety of the natural substrate. The yellow boxes show the conserved phenylalanine residues responsible for positioning of the phenyl ring of the Phe-AMP by face-to-edge hydrophobic interactions

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BMC Chemistry

ISSN: 2661-801X

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