File:CAH Bsubtilis CE7.jpg - Revision history

Joel Weadge at 19:04, 22 July 2020

2020-07-22T19:04:20Z

Joel Weadge at 18:58, 22 July 2020

2020-07-22T18:58:26Z

Joel Weadge at 18:58, 22 July 2020

2020-07-22T18:58:08Z

Joel Weadge at 18:54, 22 July 2020

2020-07-22T18:54:51Z

Joel Weadge at 18:54, 22 July 2020

2020-07-22T18:54:34Z

Joel Weadge: 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...

2020-07-22T18:53:27Z

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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.

← Older revision		Revision as of 19:04, 22 July 2020
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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.	+	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.

← Older revision		Revision as of 18:58, 22 July 2020
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−	Figure 1: CAH from B. subtilis ([{{PDBlink}}1ODS PDB ID 1ODS]). 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.	+	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.

← Older revision		Revision as of 18:58, 22 July 2020
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−	~~'''~~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.	+	Figure 1: CAH from B. subtilis ([{{PDBlink}}1ODS PDB ID 1ODS]). 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.

← Older revision		Revision as of 18:54, 22 July 2020
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−	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.	+	'''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.

← Older revision		Revision as of 18:54, 22 July 2020
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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.	+	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.