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![[Figure 4]](ud5051fig4mag.jpg)
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Figure 4
The acyl-tail binding pocket of the ECH (a), HAD (b) and KAT (c) active sites. The mode of binding of fragment M-83 (cyan) to the subsites is shown, together with the superimposed mode of binding of the acyl-CoA substrate (magenta), as predicted by model building (Dalwani et al., 2021  ). The predicted mode of binding of the acyl tail of the substrates overlaps with the fragments bound at regions E2 and E3 (residues A811 and A812), at H2 and H3 (residues A813 and A809) and at K2 and K3 (residue C508) of the three active sites. The omit mFo − DFc difference maps of these residues are shown in Table 2. Interactions of these fragments with active-site residues are visualized in Supplementary Fig. S2. |
![[Figure 4]](ud5051fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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