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Difference between revisions of "File:CAH Bsubtilis CE7.jpg"
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 | + | Figure 1. CAH from B. subtilis. A. An individual monomer from the overall CAH structure (PDB ID 1ODS) showing the α/β-hydrolase fold formed by each subunit and the β-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. |
Revision as of 11:54, 22 July 2020
Figure 1. CAH from B. subtilis. A. An individual monomer from the overall CAH structure (PDB ID 1ODS) showing the α/β-hydrolase fold formed by each subunit and the β-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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| Date/Time | Thumbnail | Dimensions | User | Comment | |
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| current | 11:53, 22 July 2020 |  | 745 × 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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