We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
Sandbox2qc8
From Proteopedia
(Difference between revisions)
(→Glutamine Synthetase: Secondary structures) |
m (→Glutamine Synthetase: Secondary structures) |
||
| Line 2: | Line 2: | ||
=Glutamine Synthetase: Secondary structures= | =Glutamine Synthetase: Secondary structures= | ||
| - | |||
| - | Glutamine synthetase is composed of 12 <scene name='Sandbox2qc8/Identical_subunits/1'>identical subunits</scene>. Each subunit is composed of 15 <scene name='Sandbox2qc8/15_alpha_helices/1'>alpha helices</scene> and 15 | ||
| - | <scene name='Sandbox2qc8/Beta_sheets/1'>beta sheets</scene>. Each subunit binds 2 Mn for a total of <scene name='Sandbox2qc8/Ligand_mn/1'>24 Mn</scene> per Glutamine Synthetase.<br> | ||
| - | |||
| - | |||
Glutamine synthetase is composed of 12 <scene name='Sandbox2qc8/Identical_subunits/1'>identical subunits</scene>. Each subunit is composed of 15 <scene name='Sandbox2qc8/15_alpha_helices/1'>alpha helices</scene> and <scene name='Sandbox2qc8/Pdb_defined_beta_strands/1'>15 beta strands</scene>. Each subunit binds 2 Mn for a total of <scene name='Sandbox2qc8/Ligand_mn/1'>24 Mn</scene> per Glutamine Synthetase.<br> | Glutamine synthetase is composed of 12 <scene name='Sandbox2qc8/Identical_subunits/1'>identical subunits</scene>. Each subunit is composed of 15 <scene name='Sandbox2qc8/15_alpha_helices/1'>alpha helices</scene> and <scene name='Sandbox2qc8/Pdb_defined_beta_strands/1'>15 beta strands</scene>. Each subunit binds 2 Mn for a total of <scene name='Sandbox2qc8/Ligand_mn/1'>24 Mn</scene> per Glutamine Synthetase.<br> | ||
Revision as of 22:16, 18 December 2008
Glutamine Synthetase: Secondary structures
Glutamine synthetase is composed of 12 . Each subunit is composed of 15 and . Each subunit binds 2 Mn for a total of per Glutamine Synthetase.
Each subunit has an exposed NH2 terminus and buried COOH terminus as part of a helical thong. [1]
The beta sheets are arranged into two separate partial beta barrels, one of which encompasses the ligand complex.
The active site within the secondary structure can be called a "bifunnel," providing access to ATP and glutamate at opposing ends.[2]
The only ligand present is a pair of Mn ions (Manganese) that indicates the active site of each subunit of the dodecamer.


