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Difference between revisions of "File:CAH Bsubtilis CE7.jpg"

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Figure 1: CAH from B. subtilis ([{{PDBlink}}1ODS PDB ID 1ODS]). A. An individual monomer from the overall CAH structure 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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Figure 1: CAH from B. subtilis ([{{PDBlink}}1ODS PDB ID 1ODS]). A) An individual monomer from the overall CAH structure 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.

Latest revision as of 11:04, 22 July 2020

Figure 1: CAH from B. subtilis (PDB ID 1ODS). A) An individual monomer from the overall CAH structure 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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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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