User:Michael Lartey/Sandbox: Difference between revisions
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At the active center of the enzyme is a glycine P-loop that connects b1 and a1 to form a giant anion hole. The hole accommodates the β-phosphoryl group of ATP, one of its natural substrates. The other natural substrate, deoxythymidine (dT), is located in the pocket formed by a3, a4 and a5. Drugs also insert into this pocket for phosphorylation. ATP binds at the giant anion hole. This active center is highly reserved in TKs. | At the active center of the enzyme is a glycine P-loop that connects b1 and a1 to form a giant anion hole. The hole accommodates the β-phosphoryl group of ATP, one of its natural substrates. The other natural substrate, deoxythymidine (dT), is located in the pocket formed by a3, a4 and a5. Drugs also insert into this pocket for phosphorylation. ATP binds at the giant anion hole. This active center is highly reserved in TKs. | ||
and display another structure. | and display another structure. | ||
{{STRUCTURE_1e2h | PDB=1e2h | SCENE= }} | {{STRUCTURE_1e2h | PDB=1e2h | SCENE= }} | ||
