Sandbox Reserved 1696

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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

Biological relevance and broader implications

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

Other features includes, mutations of D54 results in loss of INPP1 activity without changing the substrate affinity, the D54 mutant are known to trap the substrate in INPP1.

Substrate binding is largely contributed by extensive interactions involving the 1-PO4 and 4-PO4 groups. For 1-PO4, one oxygen serves as ligand for both CA1 AND CA2; another oxygen forms hydrogen bonds with main chain amide groups of S157 and T158 residues in the "DPIDST" motif.

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