Clp Protease
From Proteopedia
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| - | '''Clp protease''' (CLP) is a serine peptidase which hydrolyzes proteins in the presence of ATP and Mg+2 ion. CLP is found in mitochondria. CLP participates in degradation of misfolded proteins. CLP is a heterodimer containing an ATP-binding regulatory subunit A and catalytic subunit P. For more details see [[Clp protease]]. | + | '''Clp protease''' (CLP) is a serine peptidase which hydrolyzes proteins in the presence of ATP and Mg+2 ion. CLP is found in mitochondria. CLP participates in degradation of misfolded proteins. CLP is a heterodimer containing an ATP-binding regulatory subunit A and catalytic subunit P. For more details see <br /> |
| + | * [[Clp protease]] | ||
| + | * [[Molecular Playground/ClpP]].. | ||
==3D structures of Clp protease== | ==3D structures of Clp protease== | ||
Revision as of 11:19, 29 December 2014
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| E. coli Clp protease, 1tyf | |||||||||
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| Activity: | Endopeptidase Clp, with EC number 3.4.21.92 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Clp protease (CLP) is a serine peptidase which hydrolyzes proteins in the presence of ATP and Mg+2 ion. CLP is found in mitochondria. CLP participates in degradation of misfolded proteins. CLP is a heterodimer containing an ATP-binding regulatory subunit A and catalytic subunit P. For more details see
3D structures of Clp protease
Updated on 29-December-2014
