Sandbox Reserved 787

From Proteopedia

is an enzyme that catalyses the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle. This diagram shows the of Aconitase. The Helices are represented with blue and the sheets are represented with purple. Here we observe that the B-sheets tend to be present in the interior of the enzyme and the helices are abundant mostly on the exterior of the enzyme. are shown in yellow, we can see that there are a few anti-parallel beta-sheets at the pointed end of the enzyme and a majority of parallel beta sheets are found throughout the enzyme. The are shown in green. The are displayed in blue. We can see that the majority of the hydrophobic residues are present towards the center of the enzyme, the hydrophilic residues border the outer portion of the enzyme. The accessibility is shown here, water is represented by blue bubbles and are found on the exterior and throughout the inside of the enzyme. The ligands are labeled in purple and we can see that the water molecules interact with the ligand complex in the middle of the enzyme as water molecules are present around the ligands. The are distinguished in this image, the iron/sulfur cluster is represented by the yellow/orange complex, the Isocitric acid ligand is represented by the grey and red complex and finally the blue ball represents the oxygen. The of surrounding amino acids/residues and the substrate(Isocitric Acid) and cofactor (Iron complex) is highlighted in this image. We can see that polar charged groups (labeled blue) such as Histidine, Aspartic acid, Arginine and Glutamic acid surround the ligand. This makes sense because the ligand is surrounded by water molecules which can only be present under polar conditions. These amino acids are involved in stabilizing the bound ligand. Here the (Alanine, Histidine, Aspartic Acid and Glutamic Acid) are shown in green.