 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 7]](aso5001fig7mag.jpg)
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Figure 7
Superposition of BcSDR on its four closest structural homologs. The active-site cavity is defined by a space-filled representation of benzoic acid. The superimposed proteins (BcSDR in blue, PDB entry 6vsp from Serratia marcescens in black, PDB entry 1nff from Mycobacterium tuberculosis in cyan, PDB entry 2jah from Streptomyces clavuligerus in tan and PDB entry 4nbu from Bacillus sp. SG-1 in orange; Javidpour et al., 2014  ; MacKenzie et al., 2007; Subramanian et al., 2020; Yang et al., 2003) demonstrate the overall structural similarity and highlight the differences in the substrate-binding cavities necessary for these SDRs to catalyse their distinct chemistries. |
![[Figure 7]](aso5001fig7.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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