Sandbox Reserved 1069: Difference between revisions

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'''Binding Site A'''

Binding site A is in the center of the transmembrane domain, attached and confined via residues from the TM2 and TM5 helices. The TM2 domain has Asp45 and Asp49, and the TM5 has His153 and Asp157. The TM5 helix is significantly shorter than the other 5 helices around it, and this length forms a cavity in the membrane. In turn, this cavity is able to bind a zinc ion. This site is the protein's active site, meaning that this is where the zinc is able to attach and eventually exit the cell via proton transport. This particular site has an ideal tetrahedron among its residues which is preferred for zinc, thus making it the perfect active site for zinc to bind.

Binding site A is in the center of the transmembrane domain, attached and confined via residues from the TM2 and TM5 helices. The TM2 domain has <scene name='69/694236/Asp45/1'>Asp45</scene> and Asp49, and the TM5 has His153 and Asp157. The TM5 helix is significantly shorter than the other 5 helices around it, and this length forms a cavity in the membrane. In turn, this cavity is able to bind a zinc ion. This site is the protein's active site, meaning that this is where the zinc is able to attach and eventually exit the cell via proton transport. This particular site has an ideal tetrahedron among its residues which is preferred for zinc, thus making it the perfect active site for zinc to bind.

[[Image:Binding_site_A.fw.png|thumb|Binding Site A showing TM2 domain (left) and TM5 domain (right). The Asp45 and Asp49 as well as the His153 and Asp157 are the coordination residues in the acitve site.]]

Sandbox Reserved 1069: Difference between revisions

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@@ Line 25: / Line 25: @@
 '''Binding Site A'''
-Binding site A is in the center of the transmembrane domain, attached and confined via residues from the TM2 and TM5 helices. The TM2 domain has Asp45 and Asp49, and the TM5 has His153 and Asp157. The TM5 helix is significantly shorter than the other 5 helices around it, and this length forms a cavity in the membrane. In turn, this cavity is able to bind a zinc ion. This site is the protein's active site, meaning that this is where the zinc is able to attach and eventually exit the cell via proton transport. This particular site has an ideal tetrahedron among its residues which is preferred for zinc, thus making it the perfect active site for zinc to bind.
+Binding site A is in the center of the transmembrane domain, attached and confined via residues from the TM2 and TM5 helices. The TM2 domain has <scene name='69/694236/Asp45/1'>Asp45</scene> and Asp49, and the TM5 has His153 and Asp157. The TM5 helix is significantly shorter than the other 5 helices around it, and this length forms a cavity in the membrane. In turn, this cavity is able to bind a zinc ion. This site is the protein's active site, meaning that this is where the zinc is able to attach and eventually exit the cell via proton transport. This particular site has an ideal tetrahedron among its residues which is preferred for zinc, thus making it the perfect active site for zinc to bind.
 [[Image:Binding_site_A.fw.png|thumb|Binding Site A showing TM2 domain (left) and TM5 domain (right). The Asp45 and Asp49 as well as the His153 and Asp157 are the coordination residues in the acitve site.]]