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File:CAH Bsubtilis CE7.jpg

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Revision as of 10:53, 22 July 2020 by Joel Weadge (talk | contribs) (Figure 1. CAH from B. subtilis. A. An individual monomer from the overall CAH structure (PDB ID 1ODS) showing the a/bhydrolase fold formed by each subunit and the b-strand-like interface domain needed for association of the monomers. The catalytic tria...)
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Figure 1. CAH from B. subtilis. A. An individual monomer from the overall CAH structure (PDB ID 1ODS) showing the a/bhydrolase fold formed by each subunit and the b-strand-like interface domain needed for association of the monomers. The catalytic triad of Ser181, Asp 269 and His 298 are highlighted in cyan. B. Characteristic donut-shaped quaternary structure of the CAH hexamer. Each monomer is represented in a different colour.

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current10:53, 22 July 2020Thumbnail for version as of 10:53, 22 July 2020745 × 1,110 (178 KB)Joel Weadge (talk | contribs)Figure 1. CAH from B. subtilis. A. An individual monomer from the overall CAH structure (PDB ID 1ODS) showing the a/bhydrolase fold formed by each subunit and the b-strand-like interface domain needed for association of the monomers. The catalytic tria...

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