Birrer Sandbox 2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 9: Line 9:


The initial scene (<scene name='Birrer_Sandbox_2/Whole_adh_molecule/3'>Domains of ADH</scene>) shows an overview of the molecule, allowing for a general look at the tertiary structure of alcohol dehydrogenase (it is complexed with Cl, Pyz, NAD, and Zn). A second scene (<scene name='Birrer_Sandbox_2/Close_look_at_ligand/2'>Closer Look at Subunit</scene>) shows a close view of the ligand within each subunit. Labels have been placed on NAD, CL, and Zn to clearly establish the structure.
The initial scene (<scene name='Birrer_Sandbox_2/Whole_adh_molecule/3'>Domains of ADH</scene>) shows an overview of the molecule, allowing for a general look at the tertiary structure of alcohol dehydrogenase (it is complexed with Cl, Pyz, NAD, and Zn). A second scene (<scene name='Birrer_Sandbox_2/Close_look_at_ligand/2'>Closer Look at Subunit</scene>) shows a close view of the ligand within each subunit. Labels have been placed on NAD, CL, and Zn to clearly establish the structure.
<scene name='Birrer_Sandbox_2/The_active_site/1'>The active</scene> site of alcohol dehydrogenase has three important residues, Phe 93, Leu 57, and Leu 116. These three residues work together to bind the alcohol substrate. .<ref>''Protein: Alcohol Dehydrogenase''. The College of Saint Benedict and Saint John's University. 1 March 2010 < http://www.users.csbsju.edu/~hjakubow/classes/rasmolchime/99ch331proj/alcoholdehydro/index.htm></ref>