Sandbox Reserved 1691

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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, gene- INPP1. This enzyme is found in the organism Bos Taurus (Bovine), This enzyme functions specifically in removing a phosphate group from substate inositol. Besides that, this also functions in regulating gluconeogenesis, and sulfur assimilation. The PDB identifier of my focus is 7KIR it contains 1 ligand, and the ligand it shows is D-Myo-Inositol-1,4-Bisphosphate. The function of is dephosphorylating inositol, the substrate is IP2 and the product is IP.

Biological relevance and broader implications

Important amino acids

Inositol (1,4)-bisphosphate is a substrate that binds in the active site of INPP1D54A. The phosphate in the substrate serves as a ligand for both the calcium ions- CA1 and CA2.; Glutamic acid (290), Lysine (294), Serine (157), Threonine (158), Glutamic acid (269), and Alanine (291) largely contributed an extensive role in interactions between 1-PO4 and 4-PO4 of the substrate to the active site. ^[3]

Threonine is Amphipathic, which means it has both hydrophilic and hydrophobic parts. Serine, Threonine, and Lysine are Polar. Polar hydrophilic amino acids are important in ligand binding to the substrate because it makes the binding site precisely positioned for hydrogen bonding to the hydroxy and carboxylate groups of the substrate. Or in a different way, The charges have become important for locating or identifying the accessible area that helped the protein function. Moreover, in this article, the motif of enzymes in this family is DPIDxT, (x can be anything) but in this case, the D54, E80, E79, D153, D317, and T158. These amino acids hold the metal ions and the metals hold on to the water and substrates. The protein would not function without this holding process.

I also found that the Inotisol rings on the end have a lot to do with binding. for binding are Thr 312, Lys 270, Ala 291, Asp 156. These key amino acids are important because they participate in hydrogen bonds, hydrophobic, and ionic bonds.

of the active site with all the important amino acids

^[4].

Structural highlights

The protein is 90% transparent. The contains 77% alpha-helices, 23% beta-sheets. More specific is 13 secondary structural elements of which 10 are alpha helices and 3 are beta-sheets. Alpha helix contains 3 catalytic amino acids, and beta-sheet contains the other one catalytic acid.

Other important features

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