Sandbox Reserved 1697: Difference between revisions

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== Important amino acids==
== Important amino acids==
In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.
In the protein the ligand is <scene name='89/892740/Ligand_view/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, will be dephosphorylated by the water brought in by the magnesium ions.In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.


== Structural highlights ==
== Structural highlights ==

Revision as of 03:12, 9 December 2021

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This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699.
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7KIR

Inositol plyphosphate 1-phosphatase

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References