Introduction
This is a sample scene created with SAT to by Group, and another to make of the protein.
Overall Structure
Binding Interactions
Green 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 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. The design of this particular sulfonylpiperidine as an inhibitor. More to come.
Additional Features
Quiz Question 1
Quiz Question 2
See Also
Credits
Introduction - name of team member
Overall Structure - name of team member
Drug Binding Site - name of team member
Additional Features - name of team member
Quiz Question 1 - name of team member
Quiz Question 2 - name of team member
References
