Birrer Sandbox 2: Difference between revisions
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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. | ||
Zn plays an important role in the catalysis. It funtions by electrostatically stabilizing the oxygen in alcohol during ADH's catalysis, which causes the alcohol to be more acidic. At the <scene name='Birrer_Sandbox_2/Zinc_binding_site/1'>Zinc Binding Site</scene>, Zinc coordinates with Cys 146, Cys 174, and His 67.< http://www.users.csbsju.edu/~hjakubow/classes/rasmolchime/99ch331proj/alcoholdehydro/index.htm></ref> | Zn plays an important role in the catalysis. It funtions by electrostatically stabilizing the oxygen in alcohol during ADH's catalysis, which causes the alcohol to be more acidic. At the <scene name='Birrer_Sandbox_2/Zinc_binding_site/1'>Zinc Binding Site</scene>, Zinc coordinates with Cys 146, Cys 174, and His 67.<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> | ||
Alcohol dehydrogenase exists as a dimer with a zinc molecule complexed in each of the subunits. It has a SCOP catagory of an alpha and beta protein. It does contain at the N-terminal a domain that is all beta; however, the C-Terminal domain is alpha and beta, so the catagory is alpha and beta. The C-Terminal core has 3 layers of alpha/beta/alpha and parallel beta sheets of 6 strands.<ref>''Protein: Alcohol dehydrogenase from Human (Homo sapiens), different isozymes''. SCOP. 2009. 1 March 2010 < http://scop.berkeley.edu/data/scop.b.d.c.b.b.c.html></ref> | Alcohol dehydrogenase exists as a dimer with a zinc molecule complexed in each of the subunits. It has a SCOP catagory of an alpha and beta protein. It does contain at the N-terminal a domain that is all beta; however, the C-Terminal domain is alpha and beta, so the catagory is alpha and beta. The C-Terminal core has 3 layers of alpha/beta/alpha and parallel beta sheets of 6 strands.<ref>''Protein: Alcohol dehydrogenase from Human (Homo sapiens), different isozymes''. SCOP. 2009. 1 March 2010 < http://scop.berkeley.edu/data/scop.b.d.c.b.b.c.html></ref> | ||
