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User:Amy Kerzmann/Sandbox 5
From Proteopedia
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| - | The <scene name='User:Amy_Kerzmann/Sandbox_5/Elastase-triad/3' target='2'>elastase binding pocket</scene> contains <font color="# | + | The <scene name='User:Amy_Kerzmann/Sandbox_5/Elastase-triad/3' target='2'>elastase binding pocket</scene> contains <font color="#808080">Gly190</font>, <font color="#008000">Val216</font> and <font color="#FFA500">Thr226</font>. |
<quiz display=simple> | <quiz display=simple> | ||
Revision as of 09:04, 10 February 2010
Serine Proteases
Family includes trypsin, chymotrypsin and elastase.
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Serine proteases perform their catalytic roles using three key residues: Ser, His, Asp. Because the proteases utilize these three residues for function, they are referred to as the catalytic triad. Highlight the . Mouse over the structure to determine the residue numbers for Ser, Asp and His.
Now compare chymotrypsin to . The .
The contains Gly190, Val216 and Thr226.
