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. 2025 Jul 24;91(8):e01136-25. doi: 10.1128/aem.01136-25

Fig 5.

Phylogenetic analysis places NmCut in distinct clade among PET-degrading enzymes. Sequence alignment highlights conserved residues. Structural modeling reveals separate catalytic and binding modules, with active site forming key interactions with PET.

Structural and phylogenetic characterization of NmCut. (A) Maximum likelihood (ML) phylogenetic tree based on the amino acid sequence of NmCut and other known PET-degrading enzymes. (B) Multiple sequence alignment of NmCut with representative PETases. (C) Electrostatic surface representation of NmCut, showing a modular organization: a catalytic module (CM, orange) and a putative binding module (PBM, blue). Color scale indicates surface potential from −5.0 (red) to +5.0 (blue) kcal/mol·e. (D) Molecular docking model of NmCut with a PET trimer (green). The catalytic triad (Ser161, Asp209, His237) is shown in orange; predicted mutation sites enhancing PET interaction are indicated in blue.