Sandbox 39: Difference between revisions

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<ref>Image from:  
<ref>Image from:  
Hans-Hartwig Otto, and Tanja Schirmeister (1997) Cysteine Proteases and Their Inhibitors. Chemical Reviews. No. 97, 133-171.</ref>]]
Hans-Hartwig Otto, and Tanja Schirmeister (1997) Cysteine Proteases and Their Inhibitors. Chemical Reviews. No. 97, 133-171.</ref>]]
Specificity is controlled, however, by the <scene name='Sandbox_39/Catalytic_triad/2'>catalytic triad</scene>, a hydrophobic pocket that accommodates the side chains of the protein substrate. This triad consists of a histidine, asparagine, and a cysteine, after which the protein is categorized as a cysteine protease. Papain exhibits specific substrate preferences for hydrophobic or aromatic residues.
Specificity is controlled, however, by the <scene name='Sandbox_39/Active_site_revised/1'>catalytic diad</scene>, a hydrophobic pocket that accommodates the side chains of the protein substrate. This diad, shown above in red and clearly visible in the cleft of the enzyme, consists of cysteine25 (after which the protein is categorized as a cysteine protease)and histidine159. Papain exhibits specific substrate preferences for hydrophobic or aromatic residues.


== Secondary Structure ==
== Secondary Structure ==
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