Sandbox GGC10: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
<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 comprised of residues Val 1- Leu 6, Asp 149- Val 184, and Gln 308-Ala 326. The N-terminal is also composed of residues | <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 comprised of residues Val 1- Leu 6, Asp 149- Val 184, and Gln 308-Ala 326. The N-terminal is also composed of residues | ||
