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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

This protein is from

Biological relevance and broader implications

This protein can be found in the plant pathogenic microbe Pseudomonas syringae strain PtoDC3000. The p. syringae mutautes its host, which in this case is tomato. The p. syringae produces a toxin that cause the tomato to not be able to fight off, there for causing diseases in the tomato. This is relevant because it can affect the food supply, which as humans we need. Studying this mutant will give us an understanding on what the mutation is and if it can be avoided. The research focuses on aldehyde dehydrogenases specifically aldC. aldehyde dehydrogenases are known for its capability to detoxing aldehydes, this is important because aldehydes are very reactive, so for an example from the article they can be turned into carboxylic acids which are not as reactive, which I believe slows down the mutation.

Important amino acids

Structural highlights

The structure is made up of about 60% alpha helices and 30% beta sheets and 10% of other structures like water. the shape of this structure looks like its split in two bulbs with a narrow middle part. you can also find two ligands in each side of the structure. This is a structure to highlight the ligand of the protein while everything else is transparent. This is to show the main structure while highlighting the interaction with the ligand. There are 19 amino acids that are bind to the NAD+ ligand. The ligands that can be found in the structure are octanal and NAD+.

Other important features

NEED TO REWORD THIS The secondary structure features and domains of the AldC monomer are similar to those of other aldehyde dehydrogenase family members The C-terminal region consists of a mixed a/b domain, which includes the catalytic cysteine residue and forms the aldehyde-binding site" "The N-terminal Rossmann-fold domain contains a central b-sheet (b9-b8-b7- b10-b11) surrounded by a-helices to form the NAD(H)-binding site"