Extended Data Fig. 1: Structural comparison of SN268 (based on an Alphafold2 prediction) with its closest homolog in the PDB. | Nature Chemical Biology

Extended Data Fig. 1: Structural comparison of SN268 (based on an Alphafold2 prediction) with its closest homolog in the PDB.

From: Functional metagenomic screening identifies an unexpected β-glucuronidase

Extended Data Fig. 1

(a) Overall alignment of SN268 (green) and the β-N-acetylhexosaminidase from Akkermansia muciniphila co-crystallized with GlcNAc (PDB: 7CBO, purple). The two sequences share 40.5% identity and a high degree of structural alignment (RMSD: 0.768 Å, over 2239 atoms). (b) The focus on the active site shows an almost perfect alignment of the binding sites. A reasonable conjecture based on the perfect active site similarity is that they catalyze turnover of the same main substrate, but that weaker promiscuous activities may exist, and we have detected one of them in our droplet screens.

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