Serine protease
From Proteopedia
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- | < | + | <StructureSection load='1ppb' size='450' side='right' scene='' caption='Thrombin light chain (aqua) and heavy chain (red) complex with inhibitor (PDB code [[1ppb]])'> |
- | caption= | + | |
- | '''Serine proteases''', so called due to the presence of a serine residue in the active site, are a class of enzymes that catalyse the hydrolysis of peptide bonds in proteins. | + | '''Serine proteases''', or '''proteinases''', so called due to the presence of a serine residue in the active site, are a class of enzymes that catalyse the hydrolysis of peptide bonds in proteins. |
==Thrombin== | ==Thrombin== | ||
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The B chain consists of <scene name='Serine_Protease/Domains/1'>two domains</scene>. As is true for all of the "trypsin-like" serine proteases, each of the two thrombin domains consists mainly of a 6-stranded, antiparallel beta barrel. The specificity pocket (here filled with the Lys sidechain of the PPACK inhibitor) is in one side of the throat of the domain 2beta barrel, and the activation site is close next to it. | The B chain consists of <scene name='Serine_Protease/Domains/1'>two domains</scene>. As is true for all of the "trypsin-like" serine proteases, each of the two thrombin domains consists mainly of a 6-stranded, antiparallel beta barrel. The specificity pocket (here filled with the Lys sidechain of the PPACK inhibitor) is in one side of the throat of the domain 2beta barrel, and the activation site is close next to it. | ||
+ | ==3D structures of thrombin== | ||
+ | [[Thrombin]] | ||
- | < | + | THis is <scene name='Serine_Protease/Aapk/1'>our protein fro CHEM361</scene>. |
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- | ==Trypsin | + | ==Trypsin== |
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+ | See [[Trypsin]] | ||
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+ | ==Gilman suc-AAPK-trypsin== | ||
+ | [[2agg]] | ||
{{Clear}} | {{Clear}} |
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