Sandbox Reserved 1698

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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

The organism "Bos taurus". protein 1INP regulates inositol phosphate signaling other proteins within the family, also has roles in gluconeogenesis and nucleotide metabolism. The specific protein mentioned in the has a PDB ID of 1INP, however the protein that we will look at for ligand has PDB ID of 7KIR. This specific protein is an enzyme because its mention that it binds to substrate. It also mentions the speed of a reaction changes due to protein, and slowed down by inhibitors.

Biological relevance and broader implications

The biological relevance is that 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

This is diagram of the in the 1INP. ^[3] Electron density attribute to substrate binding. Two calcium ions (CA1 and CA2). The three metal sites in the active site of 1INP show Mg2+, Ca2+. Mg2+ in metal site are seem in the ligand interactions in both 1INP. This magnesium ions stabilize the protein and ligand to be able to catalyze the substrate.

Structural highlights

Our protein has secondary structure contains , and Also contains which is formed by the hydrophobic and non polar

Not able to see the active site due too

Other important features

Other interesting features including the mutation of D54 which results in loss of INPPL activity with changing the substrate affinity, the D54 mutant is known to trap the substrate in INPP1.

Enough though the protein 1INP doesn't have ligand, but has similar protein known as 7KIR, which contains similar catalytic amino acid. The catalytic amino acids are glutamic acid and aspartic acid, the enzyme they studied had mutation at D5, this causes amino acid alanine to become aspartic acid.

Included 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. This all the protein contributed to hydrogen bonding to the ligand.

"DPIDxT" six-amino acid motif anchor metal binding. sites likely involve catalysis

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