Sandbox GGC10: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<scene name='75/752264/Pepstatin/1'>The region of the pepstatin molecule </scene> | <scene name='75/752264/Pepstatin/1'>The region of the pepstatin molecule </scene> | ||
The region of the pepstatin molecule the residues shown. Ala,Iva, and residues as well as Sta terminal are low on density. They | The region of the pepstatin molecule the residues shown. Ala,Iva, and residues as well as Sta terminal are low on density. They must generate new conformations since the model can't fit | ||
<scene name='75/752264/Active_sites/1'>A protein inhibitor forms an extended conformation with the first hydroxyl oxygen located in the active sites between carboxyl groups Asp 32 and Asp 215 | <scene name='75/752264/Active_sites/1'>View of active sites </scene> | ||
A protein inhibitor forms an extended conformation with the first hydroxyl oxygen located in the active sites between carboxyl groups Asp 32 and Asp 215 | |||
<scene name='75/752264/Residues/1'>The structure of Human Pepsin is similar to a serine Endoproteinase with molecular weight of 35 kd. the structure is divided into 3 domains. The main domain includes 6 stranded antiparallel beta sheet that helps as a backbone to the active site region. It is | <scene name='75/752264/Residues/1'> View of residues Val 1- Leu 6, Asp 149- Val 184, and Gln 308-Ala 326 </scene> | ||
The structure of Human Pepsin is similar to a serine Endoproteinase with molecular weight of 35 kd. the structure is divided into 3 domains. The main domain includes 6 stranded antiparallel beta sheet that helps as a backbone to the active site region. It is comprisedThe N-terminal is also composed of residues | |||
Revision as of 00:18, 27 April 2018
Human Pepsin
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