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. 2025 Aug 21;5(8):101399. doi: 10.1016/j.checat.2025.101399

Figure 8.

Figure 8

Computational docking of PET model substrate in the vicinity of the catalytic triad

(A) Surface representation of PHL7-WT (green) with a bound PET model substrate (PET3mer).

(B) PET3mer substrate can be divided into three PET units (units −2, −1, +1) where unit −2 is the leaving group resulting from the esterase activity. Key residues interacting with the PET3mer, that include L210/I179 packing against the leaving group (PET unit −2), W156/F63 pi-stacking against PET unit −1 and L93/Q95 packing against PET unit +1. In this pose, Q95 is also shown to form an H-bond with the ester linkage of PET unit +1.

(C) Surface representation of PHL7-Jemez with a bound PET3mer.

(D) Key residues interacting with the PET3mer include L210/I179 (PET unit −2), W156/F63 (PET unit −1), and Y95 pi-stacking against PET unit +1. Q95Y mutation in PHL7-Jemez results in a preference of an alternate binding mode for the PET3mer substrate, especially at the PET unit +1. The catalytic triad consists of S131, D177, and H209 (cyan).