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Introduction
Structural Overview
Catalytic Triad
Ligand Binding Site
Mutations
F243
F243I
F243W
T96
T96M
T96M is located within the core of the protein. Replacing Threonine with methionine, reduces polarity as well as increasing hydrophobicity. This change leads to an overall improvement in the packing of the hydrophobic core of the protein. This mutation stabilizes the enzyme's folding, which makes it more overall resistant to higher thermodynamic conditions.
Y127
Y127G
Y127G is located in a loop near the surface of the protein. Replacing Tyrosine with a glycine increases flexibility. By replacing an aromatic bulky amino acid with the smallest amino acid, means that there is more flexibility in the loop.
N246
S283 & D238
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
