Kisker lab: 5B5Q: Difference between revisions
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<StructureSection load='' size='540' side='right' caption='Caption for this structure' scene='78/781027/Panela/3'> | <StructureSection load='' size='540' side='right' caption='Caption for this structure' scene='78/781027/Panela/3'> | ||
===Fold=== | ===Fold=== | ||
<scene name='78/781027/Panela/3'>Panel A:</scene> The overall structure, shown as cartoon, has a fold common to other deubiquitinases (green) with a helix inserted between strand 1 and 2 (yellow). The protein belongs to the family of cysteine proteases, in which an active-site cysteine initiates hydrolysis by acting as a nucleophile. Just like serine proteases, cystein proteases have a catalytic triad (i.e. three highly conserved residues in the active site). The catalytic triad is shown in all-bonds representation. | <scene name='78/781027/Panela/3'>Panel A:</scene> The overall structure, shown as cartoon, has a fold common to other deubiquitinases (green) with a helix inserted between strand 1 and 2 (yellow). The protein belongs to the family of cysteine proteases, in which an active-site cysteine initiates hydrolysis by acting as a nucleophile. Just like serine proteases, cystein proteases have a catalytic triad (i.e. three highly conserved residues in the active site). The catalytic triad is shown in all-bonds representation. [[protease]] | ||