Sandbox Reserved 1852: Difference between revisions

Line 30:

: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.

Residue 284 resides deep within the binding pocket of the enzyme. The group chose a<scene name='10/1075253/S284/2'>serine</scene> to <scene name='10/1075253/A285_scence/2'>alanine</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.

=====A285N=====

:<scene name='10/1075254/N285/3'>N285</scene>, as follows, is also buried within the binding pocket. The group introduced this mutation to increase steric hindrance with the catalytic tyrosine, reducing the number of rotamers the residue has to increase the reactivity of the enzyme by lowering the distance between Y134 and the ligand.

Sandbox Reserved 1852: Difference between revisions

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@@ Line 30: / Line 30: @@
 :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.
+Residue 284 resides deep within the binding pocket of the enzyme. The group chose a<scene name='10/1075253/S284/2'>serine</scene> to <scene name='10/1075253/A285_scence/2'>alanine</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.
 =====A285N=====
 :<scene name='10/1075254/N285/3'>N285</scene>, as follows, is also buried within the binding pocket. The group introduced this mutation to increase steric hindrance with the catalytic tyrosine, reducing the number of rotamers the residue has to increase the reactivity of the enzyme by lowering the distance between Y134 and the ligand.