Fig. 4: Structure and sequence characteristics of APET enzymes and known PETases. | Nature Communications

Fig. 4: Structure and sequence characteristics of APET enzymes and known PETases.

From: Harnessing protein language model for structure-based discovery of highly efficient and robust PET hydrolases

Fig. 4

a Crystal structure of KbPETase (green, PDB: 9IW9) and IsPETase (blue, PDB: 5XH3). The substrate structure (yellow) is derived from the IsPETase structure and structurally aligned with the KbPETase pocket. Pocket structure of (b) IsPETase and (c) KbPETase. d Phylogenetic tree of the 34 candidate proteins selected for experimental validation (blue and green) alongside previously reported PETases (orange). The APET candidates with confirmed activity are marked with green, otherwise in blue. (e, f) Sequence logo plots for the pocket residues. The height of each letter indicates the conservation score for each site, indexed by the residue position in KbPETase, with catalytic traid marked in red. g Structure-based alignment of pocket residues from APET (green) and known PETases (orange). Residues are annotated by their biochemical properties, with hierarchical clustering presented on the right. Residue indices correspond to their positions in KbPETase.

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