Sandbox 172: Difference between revisions
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<scene name='Sandbox_172/Residue1/6'>Ser 603</scene>-denoted in black, may have functional significance, there has been no observed interaction of Ser 603 with glucose substrates. A torsional rotation of of the hydroxyl group brings about a much better distance for hydrogen bonding of the glucose O6. As a result of this observation, it can be assumed that Ser 603 may have some transient role during [http://en.wikipedia.org/wiki/phosphorylation phosphorylation].<ref name="one" /> | <scene name='Sandbox_172/Residue1/6'>Ser 603</scene>-denoted in black, may have functional significance, there has been no observed interaction of Ser 603 with glucose substrates. A torsional rotation of of the hydroxyl group brings about a much better distance for hydrogen bonding of the glucose O6. As a result of this observation, it can be assumed that Ser 603 may have some transient role during [http://en.wikipedia.org/wiki/phosphorylation phosphorylation].<ref name="one" /> | ||
===Regulatory Binding Site=== | ===Regulatory Binding Site=== | ||
As glucose-6-phosphate is being produced it binds to either one of the domains on hexokinase type I. On domain 1, the phosphate moiety is surrounded by Ser 88, Thr 232, and Ser 415. The presence of these three residues generate an anion binding site that is approximately 5.6 Å to the 6 hydroxyl of the glucose that is bound.<ref name="one" /> | As glucose-6-phosphate is being produced it binds to either one of the domains on hexokinase type I. On domain 1, the phosphate moiety is surrounded by <scene name='Sandbox_172/Residue1/7'>Ser 88, Thr 232, and Ser 415</scene>. The presence of these three residues generate an anion binding site that is approximately 5.6 Å to the 6 hydroxyl of the glucose that is bound.<ref name="one" /> | ||
