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| Human Glutamine Synthetase Tertiary Structure: Pfam domains
| | <applet load='2ktq.pdb' size='300' frame='true' align='right' caption='Klentaq1–Open conformation' scene= 'Sandbox_dvoet/DNA_polymerase/Klentaq1-open_conformation/2'/> |
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| The active site of Glutamine synthetase is the result of the interactions between two adjacent subunits.
| | Here, Klentaq1's N-terminal, palm, fingers and thumb domains are yellow, magenta, green, and blue, respectively. The DNA is drawn in stick form colored according to atom type (template C cyan, primer C green, N blue, O red, and P orange). The primer's 3' ddC residue is shown in space-filling form as is the bound ddCTP, in which is C yellow. |
| 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.
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| Beta Grasp domain (N-terminus)
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| -comprised of residues 43-123
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| -binds glutamate, ammonia, and ATP
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| <show protein alignment image>
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| <show structure of the domain in viewer>
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| Catalytic domain (C-terminus)
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| -comprised of residues 129-382
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| -how it functions is not described, more research is necessary here
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| <show alignment image>
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| <show structure of the domain in viewer>
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| Active site
| | <scene name='Sandbox_dvoet/DNA_polymerase/Morphtest1/1'>morph test scene</scene> |
| -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.
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| <show relation between chains, domains, and active sites with viewer> | |
| -describe visually the important aspects of the active site
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| <show active site and ligands relationship, may need multiple scenes> | |
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