Sandbox Reserved 703: Difference between revisions

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The <scene name='Sandbox_Reserved_703/Active_center/1'>active site</scene> is similar to other phosphate SBPs.
The <scene name='Sandbox_Reserved_703/Active_center/1'>active site</scene> is similar to other phosphate SBPs.
The surface of the binding pocket is negative.  
The surface of the binding pocket is negative.  
In total, 8 residues and 13 hydrogen bonds are involved in the binding of the substrate creating a rich network. 12 bonds are formed by dipolar donor groups with 6 backbones NHs (T8, L9, S32, S144, G145, T146) mostly located at the end of 3 helices, 2 NH side chains from R140 and 4 from side chains OHs (T8, S32, S144, T146)
In total, 8 residues and 13 hydrogen bonds are involved in the binding of the substrate creating a rich network. 12 bonds are formed by dipolar donor groups with <scene name='Sandbox_Reserved_703/6n_backbones/1'>6 backbones NHs</scene> (T8, L9, S32, S144, G145, T146) mostly located at the end of 3 helices, 2 NH side chains from R140 and 4 from side chains OHs (T8, S32, S144, T146)


R140 generates two hydrogen bonds with both negative oxygen atoms of the dibasic phosphate. This interaction, by diminishing the charge coupling interaction between the guanidium and phosphate, has previously been described as essential for the fast release of the ionic substrate bound with charged residues.
R140 generates two hydrogen bonds with both negative oxygen atoms of the dibasic phosphate. This interaction, by diminishing the charge coupling interaction between the guanidium and phosphate, has previously been described as essential for the fast release of the ionic substrate bound with charged residues.

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OCA, Christine Ponkratz