Sandbox Reserved 1696

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

The protein of 1INP regulates inositol phosphate signaling other protein within the family also have roles in gluconeogenesis and nucleotide. The protein that will be looking at for the ligand has a PDB ID of 7KIR.Our organism is Bos taurus.

Biological relevance and broader implications

Many organisms have the same enzyme and they chose to use it from cows. If they can see the importance of 7KIR in IP3 inhibition, they can better understand the metabolic pathway.

Important amino acids

are an important part of the drug binding site ^[3].

The protein 1INP does not have a ligand, however, in the paper, the crystalline study shows other similar proteins, protein such as 7KIR, has similar catalytic amino acids.

The catalytic amino acids are glutamic acid, and aspartic acid, the enzyme had a mutation at DD54, which causes the alanine changed to aspartic acid.

The protein has catalytic amino acid, such as Thr 312, LYS 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, and Thr 313.All these proteins are involved in hydrogen bond to the ligand.

Catalytic amino acids in an enzyme are located in the active center responsible for accelerating enzyme catalyzed reactions, catalytic triads are a set of three coordinated amino acids that can be found in the active site of some enzymes.

Structural highlights

Other important features

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.