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![[Figure 3]](hv5064fig3mag.jpg)
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Figure 3
Active site of HCHL, into which the natural substrate feruloyl-CoA has been modelled. The active site is at the interface between monomer A (red) and monomer B (blue). In the foreground, interactions between the side chains of AMet70, ATyr75 and BTyr239 and the aromatic ring of feruloyl-CoA can be seen. BTyr239 is shown making a hydrogen bond (dashed line) to the phenolic hydroxyl of the substrate. The carbonyl group of the thioester of coenzyme A is bound in the oxyanion hole formed by the peptidic NH groups of Met70 and Gly120 (indicated by dashed lines). A structural water, W748, is shown coordinated to both Glu143 and the NH group of Gly151 (indicated by dashed lines) and was at a distance of 3.3 Å from the benzylic C atom in the model. |
![[Figure 3]](hv5064fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
