Sandbox Reserved 1756

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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 specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of two substrates, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

Biological relevance and broader implications

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

Important amino acids

are an important parts of the ligands binding site ^[3].

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

Structural highlights

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An ornithine aminotransferase is composed of 50% of alpha helices, 45% of beta sheets, and 5% of other structures.

The beta sheet contains 1 of the 3 catalytic amino acids.