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![[Figure 2]](hv5064fig2mag.jpg)
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Figure 2
(a) Structure of HCHL monomer. The N-terminal domain is shown in red and the C-terminal domain in blue. Residue side chains that form salt bridges that stabilize the domain interactions between Asp129 and Lys220 and between Arg227 and Asp160 are shown as cylinders. (b) Side view of the HCHL hexamer illustrating monomers A (red), B (blue), C (green), D (cyan), E (yellow) and F (magenta). (c) Semi-transparent surface model of HCHL with underlying ribbons of monomer A (light blue) and B (pink) showing modelled coenzyme A ferulic acid ester [3-(4-hydroxy-3-methoxy-phenyl)prop-2-enoic acid, yellow) in the active-site cleft at the monomer interface. |
![[Figure 2]](hv5064fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
