Sandbox Reserved 804

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This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807.

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spinqualitylabelsall models TRIOSEPHOSPHATE ISOMERASE Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Triose phosphate isomerase (TIM) is an enzyme that catalyzes the reaction of D-glyceraldehyde 3-phosphate to glycerone phosphate. It binds with the ligand 2-Phosphoglycolic acid (PGA).This is the of TIM.

This is in TIM.

This is the . The indigo represents the alpha helices and the violet represents the beta sheets. The structure is an alpha-beta-alpha conformation. The beta barrel is antiparallel and is surrounded by alpha helices which act to turn the sequence.

This is the secondary structure of TIM with interactions between the backbone. H Bonds are depicted in orange. Disulfide bonds should be represented in black in this structure but they are not seen. Most of the hydrogen bonds are present within the secondary structures of the alpha helices and beta barrels.

This image depicts the within TIM and they are shown in grey. The are displayed in blue. Ignore the hydrophilic interactions shown floating above the structure because they represent the hydrophilic interactions in chain B. The hydrophobic interactions are within the protein while the hydrophilic interactions are on the outside/surface of the protein.

The is located between the alpha helices and the beta sheets. The molecules form a diagonal line and are near where the monomers connect for dimer formation.

PGA is the ligand that binds TIM. is displayed in yellow. Its binding catalyzes the reaction of D-glyceraldehyde 3-phosphate to glycerone phosphate.

The are displayed in red, white, and blue. Red represent anionic side chains, the blue represent cationic side chains, and the white resemble nonpolar side chains. The ligand contacts make sense as both anionic and cationic residues are present to interact with the ligand.