Sandbox Reserved 1852: Difference between revisions

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DA_20_10 provided key mutations in and around the active site that increased the hydrophobicity, provided structural stability, and increased interactions between the ligand and surrounding residues.

=====Q162R=====

:Residue 162, a <scene name='10/1075254/Q162/1'>glutamine</scene>, resides near the top of the binding entrance to the enzyme, and is outside 3 Angstroms in most models on the enzyme. It can act as a hydrogen bond donor to the terminal phosphate on the ligand when in proximity. To increase this interaction, the group chose to mutate this Q to an <scene name='10/1075254/Q_to_r/1'>arginine</scene>, which decreased the length of the potential hydrogen bond to within 2.5 Angstroms, increasing the strength of the interaction.

:Residue 162, a <scene name='10/1075254/Q162/2'>glutamine</scene>, resides near the top of the binding entrance to the enzyme, and is outside 3 Angstroms in most models on the enzyme. It can act as a hydrogen bond donor to the terminal phosphate on the ligand when in proximity. To increase this interaction, the group chose to mutate this Q to an <scene name='10/1075254/Q_to_r/1'>arginine</scene>, which decreased the length of the potential hydrogen bond to within 2.5 Angstroms, increasing the strength of the interaction.

=====S284A=====

Residue 284 resides deep within the binding pocket of the enzyme. The group chose an <scene name='10/1075253/S284/2'>S</scene> to <scene name='10/1075253/A285_scence/2'>A</scene> mutation to increase the hydrophobicity of the binding pocket and reduce reactivity, without also changing any steric characteristics in the region ''unintentionally'' near the catalytic residues.

Sandbox Reserved 1852: Difference between revisions

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@@ Line 28: / Line 28: @@
 DA_20_10 provided key mutations in and around the active site that increased the hydrophobicity, provided structural stability, and increased interactions between the ligand and surrounding residues.
 =====Q162R=====
-:Residue 162, a <scene name='10/1075254/Q162/1'>glutamine</scene>, resides near the top of the binding entrance to the enzyme, and is outside 3 Angstroms in most models on the enzyme. It can act as a hydrogen bond donor to the terminal phosphate on the ligand when in proximity. To increase this interaction, the group chose to mutate this Q to an <scene name='10/1075254/Q_to_r/1'>arginine</scene>, which decreased the length  of the potential hydrogen bond to within 2.5 Angstroms, increasing the strength of the interaction.
+:Residue 162, a <scene name='10/1075254/Q162/2'>glutamine</scene>, resides near the top of the binding entrance to the enzyme, and is outside 3 Angstroms in most models on the enzyme. It can act as a hydrogen bond donor to the terminal phosphate on the ligand when in proximity. To increase this interaction, the group chose to mutate this Q to an <scene name='10/1075254/Q_to_r/1'>arginine</scene>, which decreased the length  of the potential hydrogen bond to within 2.5 Angstroms, increasing the strength of the interaction.
 =====S284A=====
 Residue 284 resides deep within the binding pocket of the enzyme. The group chose an <scene name='10/1075253/S284/2'>S</scene> to <scene name='10/1075253/A285_scence/2'>A</scene> mutation to increase the hydrophobicity of the binding pocket and reduce reactivity, without also changing any steric characteristics in the region ''unintentionally'' near the catalytic residues.