Sandbox Reserved 1697

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 function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are .

Biological relevance and broader implications

Important amino acids

In the protein seen in the paper there is a mutation at residue 54, causing an . The catalytic amino acids are Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313.

Structural highlights

This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is , the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions.

Other important features

The ligand of the protein is known as , with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.

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.