Sandbox Reserved 432
From Proteopedia
(Difference between revisions)
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==Binding Interactions== | ==Binding Interactions== | ||
| - | Green scene <scene name='48/483889/Actiive_site_ros/1'>Activesite</scene> gives a rough outline of the TMK backbone and a look at its active site. Outlined, in ball and stick model, are the active site residues as well as the bound sulfonylpiperidine ligand. The key residues are Arg 48, Phe 66, Ser 97, and Gln 101. In green scene <scene name='48/483889/Actiive_site_ros/2'>Interactions</scene> you are able to see that Arg 48, Ser 97, and Gln 101 form hydrogen bonds with the sulfonylpiperidine ligand. The hydrogen bond locations are shown with distances between the atoms which hydrogen bond with each other in one of the subunits. Arg 48 in particular forms one hydrogen bond with the phenolic group on the ligand. The ligand's ability to hydrogen bond with this particular residue was crucial because Arg 48 is a highly conserved residue. In other words it is seen in the active site in other TMK organisms. Moreover the hydrogen bond with Arg 48 is necessary in order for the ligand to have high enzyme affinity. | + | Green scene <scene name='48/483889/Actiive_site_ros/1'>Activesite</scene> gives a rough outline of the TMK backbone and a look at its active site. Outlined, in ball and stick model, are the active site residues as well as the bound sulfonylpiperidine ligand. The key residues are Arg 48, Phe 66, Ser 97, and Gln 101. In green scene <scene name='48/483889/Actiive_site_ros/2'>Interactions</scene> you are able to see that Arg 48, Ser 97, and Gln 101 form hydrogen bonds with the sulfonylpiperidine ligand. The hydrogen bond locations are shown with distances between the atoms which hydrogen bond with each other in one of the subunits. Arg 48 in particular forms one hydrogen bond with the phenolic group on the ligand. The ligand's ability to hydrogen bond with this particular residue was crucial because Arg 48 is a highly conserved residue. In other words it is seen in the active site in other TMK organisms. Moreover the hydrogen bond with Arg 48 is necessary in order for the ligand to have high enzyme affinity. If this sulfonylpiperidine is able to hydrogen bond with Arg 48, it will also be able to have relatively high binding affinity to the TMK of other oganisms. Will edit as other sections are added. |
==Additional Features== | ==Additional Features== | ||
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Overall Structure - name of team member | Overall Structure - name of team member | ||
| - | Drug Binding Site - | + | Drug Binding Site - Ross Furash |
Additional Features - name of team member | Additional Features - name of team member | ||
Revision as of 16:32, 9 March 2015
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
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