Sandbox1

Human Glutamine Synthetase Tertiary Structure: Pfam domains

The active site of Glutamine synthetase is the result of the interactions between two adjacent subunits. Each Subunits contains two two ends, the C-terminus and the N-terminus. The Glutamine synthetase beta grasp domain(N-terminus), and the Glutamine synthetase catalytic domain (the C-terminus). In order to stabilize the molecule, the two domains are involved in the Van Der Walls , Hydrogen . The Beta Grasp domain interact with the C-terminus of the next subunit.the two domains are proceeded by a meander of 3-24 residues that link the chains in the proteins core.

Beta Grasp domain (N-terminus) -comprised of residues 43-123 -binds glutamate, ammonia, and ATP <show protein alignment image> <show structure of the domain in viewer>

Catalytic domain (C-terminus) -comprised of residues 129-382 -how it functions is not described, more research is necessary here

<show alignment image> <show structure of the domain in viewer>

Active site -there are 10 active sites in the decamer of the protein, each formed from the beta grasp domain of one chain and the catalytic domain of the neighboring chain. <show relation between chains, domains, and active sites with viewer> -describe visually the important aspects of the active site <show active site and ligands relationship, may need multiple scenes>

---