Figure 3 | Scientific Reports

Figure 3

From: Towards a general approach for tailoring the hydrophobic binding site of phenylalanine ammonia-lyases

Figure 3

2-Methoxycinnamic acid 2c docked into the active site of: (A) wt-RtPAL (green, − 4.2 kcal/mol), L134A RtPAL (purple, − 6.9 kcal/mol), and H137F/Q138L/L266V RtPAL (grey, − 8 kcal/mol); (B) wt-PcPAL (green, − 7.3 kcal/mol) and L134A PcPAL (purple, − 7.7 kcal/mol). Steric clashes between the ortho-methoxy group and side chains of residues L266 and L134, respectively, are highlighted with red dashed lines. The modified residues and the active site orientation of 2c within the corresponding PAL variant is marked with similar colour.

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