Sandbox Reserved 785

From Proteopedia

is an enzyme used in the citric acid cycle to catalyze the oxidation of malate to oxaloacetate. Variations of this enzyme come from numerous organisms. The variation shown here is from the bacterium Bacillus anthracis. The of this enzyme consist of alpha helices (red) and beta sheets (orange). in the backbone (green) show that the beta sheets (orange) are arranged in parallel in the protein since the hydrogen bonds are angled, not straight, between the sheets. When looking at malate dehydrogenase in ball and stick form the (grey) are contained primarily in the center of the polypeptide, while the hydrophilic residues (cyan) are primarily toward the outside of the molecule. Primarily the the outer portions of the polypeptide are much more accessible to (water) than the inner portions since the water molecules (blue) mostly congregate on the outside of the protein (white), though it is worth noting some solvent does reach the active sites. The sites on the enzyme that are either cationic (blue) or anionic (red). These charged residues allow for interactions with the ligands so that they are attracted to, and bind in the proper area. The which make contact with these residues (lime green) include the substrate and cofactors relevant to the function of the enzyme. The (pink) are are those specifically functioning in the active sites of the protein.