Sandbox Reserved 1670

Text To Be Displayed

This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682.

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Structure of Aldehyde dehydrogenase

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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 or to the article describing Jmol to the rescue. Structural highlights Mutated Catalytic Tetrad Protein Structure Catalytic Tetrad NAD and Octanal 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. ligands 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"