Sandbox 5: Difference between revisions
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== The Oxygenase domain of NOS == | == The Oxygenase domain of NOS == | ||
{{STRUCTURE_2g6h|PDB=2g6h|SCENE=Sandbox_5/Nos_oxygenase_med_cofaktore/3}} | |||
The <scene name='Sandbox_5/Nos_oxygenase_med_cofaktore/3'>oxygenase domain</scene> contains the active site of the enzyme. The active site binds the substrate L-<scene name='Sandbox_5/Nos_oxygenase_arg/2'>Arginine</scene> ([http://en.wikipedia.org/wiki/Arginine Arginine]) and is converted into citruline and NO (explained in details below). The domain has three cofactors bound: | The <scene name='Sandbox_5/Nos_oxygenase_med_cofaktore/3'>oxygenase domain</scene> contains the active site of the enzyme. The active site binds the substrate L-<scene name='Sandbox_5/Nos_oxygenase_arg/2'>Arginine</scene> ([http://en.wikipedia.org/wiki/Arginine Arginine]) and is converted into citruline and NO (explained in details below). The domain has three cofactors bound: | ||
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and a Zinc ion. | and a Zinc ion. | ||
General Structure | |||
The oxygenase domain can also be divided into three subdomains. Firstly, the substrate-binding subdomain, which is crescent in shape, binds the substrate in an interior pocket of the crescent. The Heme group is located between the tips of the crescent shape, thus closing the pocket in which the substrate is located. Secondly the the BH4 binding subdomain serves as a cap for the for the cavity created by the substrate binding domain's crescent shape. Thirdly there is a subdomain with two helical bundles making up a hydrophobic core, however this subdomain is not thought to take part of the enzymatic activity of NOS. | The oxygenase domain can also be divided into three subdomains. Firstly, the substrate-binding subdomain, which is crescent in shape, binds the substrate in an interior pocket of the crescent. The Heme group is located between the tips of the crescent shape, thus closing the pocket in which the substrate is located. Secondly the the BH4 binding subdomain serves as a cap for the for the cavity created by the substrate binding domain's crescent shape. Thirdly there is a subdomain with two helical bundles making up a hydrophobic core, however this subdomain is not thought to take part of the enzymatic activity of NOS. | ||
