Sandbox 172: Difference between revisions

===Glucose Binding Sites===

The residues of the glucose binding site of Hexokinase Type I are very highly conserved within the hexokinase sequence; glucose binds equally to both domains or "lobes" of the structure. As a result, hexokinase type I in its native conformation has an active site in its inactive regulatory domains. Before glucose binds to hexokinase type I, it is said to be in an open conformation. ATP is already bound within one of the domains but it is situated a distance from the glucose binding site. As the glucose binds, the two domains close around the glucose substrate and this change results in a newly formed pattern of hydrogen bonding.

===Active Site===

In the <scene name='Sandbox_172/Mynewscene/2'>active site</scene> of hexokinase type I, Lys 621 and Asp 657 show the hydrogen-bonding distance in which a reactive O6 hydroxyl is situated in between.