Journal:Acta Cryst F:S2053230X22007555
From Proteopedia
(Difference between revisions)
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<jmol><jmolButton><script>frame 1 1 play; animation off; frame 1</script><text>only EmGluRS</text></jmolButton><jmolButton><script>frame 2 2 play; animation off; frame 2</script><text>only EaGluRS</text></jmolButton><jmolButton><script>animation off; frame all</script><text>both EmGluRS and EaGluRS</text></jmolButton></jmol> | <jmol><jmolButton><script>frame 1 1 play; animation off; frame 1</script><text>only EmGluRS</text></jmolButton><jmolButton><script>frame 2 2 play; animation off; frame 2</script><text>only EaGluRS</text></jmolButton><jmolButton><script>animation off; frame all</script><text>both EmGluRS and EaGluRS</text></jmolButton></jmol> | ||
| - | EmGluRS shares ~97% sequence identity with EaGluRS but less than 39% sequence identity with any other structures in the Protein Data Bank. EmGluRS and EaGluRS have prototypical bacterial GluRS topology. EmGluRS and EaGluRS have similar binding sites and tertiary structures to other bacterial GluRS that are promising drug targets. These structural similarities can be exploited for drug discovery. <scene name='91/917942/Cv/ | + | EmGluRS shares ~97% sequence identity with EaGluRS but less than 39% sequence identity with any other structures in the Protein Data Bank. EmGluRS and EaGluRS have prototypical bacterial GluRS topology. EmGluRS and EaGluRS have similar binding sites and tertiary structures to other bacterial GluRS that are promising drug targets. These structural similarities can be exploited for drug discovery. <scene name='91/917942/Cv/6'>Test</scene> |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 15:17, 27 July 2022
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
