Sandbox Reserved 1694

This is a default text for your page Sandbox 1677. Click above on edit this page to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Function of your protein

Inositol polyphosphate 1-Phosphatase (INPP1) is an enzyme that removes a phosphate group from a substrate through hydrolysis. Specifically, the phosphomonoester bond is removed from position 1 phosphate of Ins(1,4)P2 or Ins(1,3,4)P3. This enzyme is found in the organism Bovine.

Biological relevance and broader implications

This enzyme also helps to regulate gluconeogenesis and nucleotide metabolism and

Important amino acids

These play an extensive role in interactions between 1-PO4 and 2-PO4 of the substrate to the active site. Also, there are a few different that interact with the inositol ring and help reinforce the binding of the Ins(1,4)P2. ^[3]

Structural highlights

INPP1D54A contains 13 secondary structural elements of which 10 are alpha helices and 3 are beta-sheets (). Percentage-wise, I would predict the protein is 77% alpha-helices, 23% beta-sheets. Alpha helix 8 and beta-sheet 2 each contain one catalytic amino acid. Also, helix 6 and 7 and beta-sheet 2 form important interactions with the substrate (have 6 of the 9 amino acids that interact with the substrate).

Inositol (1,4)-bisphosphate is a that binds in the active site of INPP1D54A. The phosphate (1-PO4) in the substrate serves as a ligand for both the calcium ions. ^[3]

Other important features

In the structure INPP1D54A, there is a mutation in the amino acid aspartic acid (D)54 and causes it to change to alanine (A)54 (). This mutation does not impact the substrate affinity but does decrease the activity of INPP1. ^[3]

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.