FirstGlance/Visualizing Conservation: Difference between revisions
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[[Image:6cqz-consurf-vx-contacts-shown.gif]] | [[Image:6cqz-consurf-vx-contacts-shown.gif]] | ||
</td></tr></table> | </td></tr></table> | ||
'''Conclusions:''' Ser203 is covalently bonded to the phosphorus in VX. His447 (3.4 Å) and Gly121 (2.9 Å) are likely [[Hydrogen bonds|hydrogen-bonded]] to oxygens in VX. | |||
For instructions on how to measure a distance, click ''Distances/Angles'' in the Tools tab. You can later return to the Contacts Shown controls by clicking ''Return to Contacts'' which will appear in the middle left next to ''ConSurf Colors''. | |||
In human acetylcholinesterase, the catalytic triad residues<ref>PMID: 24900610</ref> are Ser203, His447, and Glu334. We can see that the first two are highly conserved, but what about Glu334 which is not contacting VX? | |||
==Conservation of Protein Crosslinks== | ==Conservation of Protein Crosslinks== | ||
