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Human Glutamine Synthetase Tertiary Structure: Pfam domains | |||
-(describe structure of protein leading in to a single chain) | |||
-each chain contains 2 domains, 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> | |||