 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 5]](aso5001fig5mag.jpg)
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Figure 5
Active site of BcSDR. The active site of BcSDR (yellow C atoms) in complex with benzoic acid (green C atoms) is shown in (a). Water molecules are represented as red spheres. Hydrogen bonds are illustrated with black lines and bond distances are given in Å. O atoms are shown in red and N atoms are shown in blue. BcSDR and a B. multivorans SDR with the active-site Leu144 (yellow) and Tyr159 (pink) residues overlaid (b) reveal a similar environment between the water molecule and the O atom of Tyr159. Because BcSDR does not have the conserved tyrosine of classical SDRs, it is likely that Ser131 or Asn83 (c) would act as the general base in the enzyme mechanism. |
![[Figure 5]](aso5001fig5.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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