 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 5]](va5051fig5mag.jpg)
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Figure 5
Multiple structure-based sequence alignment of SmTetX with the tetracycline destructases TetX from B. thetaiotaomicron (PDB entry 2y6r; Volkers et al., 2011  ) and Tet(50) (PDB entry 5tue; Park et al., 2017), and the putative reductase AbsH3 from Streptomyces sp. (PDB entry 6n04; Clinger et al., 2021). Regions significant for the re site of the enzyme are shown. The key residues in the binding pocket of SmTetX are highlighted by a black background (and shown in Fig. 4). Identity, similarity and dissimilarity of the key amino acids are marked with green, orange and red backgrounds, respectively. *The sequence and structure of this region are the same for TetX, TetX2, TetX4 and TetX7 (Cheng et al., 2022). |
![[Figure 5]](va5051fig5.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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