Sandbox Reserved 1077: Difference between revisions
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The <scene name='69/694244/Secondary_structure/1'>secondary structure</scene> of this enzyme is typical of α/β hydrolases | The <scene name='69/694244/Secondary_structure/1'>secondary structure</scene> of this enzyme is typical of α/β hydrolases | ||
The structure solved by x-ray crystallography was missing the <scene name='69/694244/Glu38/1'>N-terminal</scene> 37 residues as well as a <scene name='69/694244/Glu193_and_arg205/3'>flexible loop</scene> (residues 194-204). | The structure solved by x-ray crystallography<ref>PMID:21637775</ref> was missing the <scene name='69/694244/Glu38/1'>N-terminal</scene> 37 residues as well as a <scene name='69/694244/Glu193_and_arg205/3'>flexible loop</scene> (residues 194-204). | ||
Revision as of 02:21, 1 April 2015
This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080. |
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Rv0045c hydrolase from M. TuberculosisRv0045c hydrolase from M. Tuberculosis
FunctionDiseaseRelevanceStructural highlightsThe of this enzyme is typical of α/β hydrolases The structure solved by x-ray crystallography[1] was missing the 37 residues as well as a (residues 194-204).
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ReferencesReferences
- ↑ Zheng X, Guo J, Xu L, Li H, Zhang D, Zhang K, Sun F, Wen T, Liu S, Pang H. Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis. PLoS One. 2011;6(5):e20506. Epub 2011 May 26. PMID:21637775 doi:10.1371/journal.pone.0020506