Sandbox Reserved 1670

This is a default text for your page '. 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

Disease

Relevance

plant mutations

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+.

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"