SCP2-thiolase

Structure of the zebrafish SCP2-thiolase

spinqualitylabelsall models This is the asymmetric unit 1.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D The SCP2-thiolase is a member of the thiolase family of enzymes. It has low sequence identity with any of the other thiolases. Like many other thiolases it is a dimer in solution. In the 6HSP crystal structure there are two monomers per asymmetric unit. One monomer forms the classical dimer with a two-fold related symmetry mate. The other monomer has a different packing and it is not forming the classical dimer: its structure is the structure of the monomer. There are large structural differences between these two monomers. The comparison of the structures of the "dimerised" monomer and the single monomer visualises the structural changes that happen when the single monomer dimerises to form the mature dimer. The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related symmetry copy. The active site is at the dimer interface The active site is shaped by the residues of four loops Function Here something about function Structural highlights morph This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Proteopedia Page Contributors and Editors (what is this?)

Rik Wierenga, Michal Harel