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E. coli Clp protease, 1tyf
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Activity:
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Endopeptidase Clp, with EC number 3.4.21.92
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Structural annotation:
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Resources:
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CATH : 1Tyfa00, 1Tyfb00, 1Tyfc00, 1Tyfd00, 1Tyfe00, 1Tyff00, 1Tyfg00, 1Tyfh00, 1Tyfi00, 1Tyfj00, 1Tyfk00, 1Tyfl00, 1Tyfm00, 1Tyfn00 InterPro : Ipr001907 Pfam : PF00574 SCOP : d1tyfa_, d1tyfb_, d1tyfc_, d1tyfd_, d1tyfe_, d1tyff_, d1tyfg_, d1tyfh_, d1tyfi_, d1tyfj_, d1tyfk_, d1tyfl_, d1tyfm_, d1tyfn_ UniProt : P0A6G7
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Resources:
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FirstGlance, OCA, PDBsum, RCSB
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Coordinates:
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save as pdb, mmCIF, xml
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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.
3D structures of Clp protease3D structures of Clp protease
Updated on 20-November-2014
{"openlevels":0}
- CLP P subunit
- 1tyf, 1yg6 – EcCLP – Escherichia coli
- 1yg8, 3hln - EcCLP (mutant)
- 1y7o – CLP – Streptococcus pneumoniae
- 1tg6 - CLP – human
- 2f6i, 4gm2, 4hnk - CLP – Plasmodium falciparum
- 2cby, 2ce3, 2c8t - CLP – Mycobacterium tuberculosis
- 3fes - CLP – Clostridium difficile
- 3ktg, 3kth, 3tt6 – BsCLP – Bacillus subtilis
- 3p2l - CLP – Francisella tulerensis
- 3q7h - CLP – Coxiella burnetii
- 3qwd, 3st9, 3sta, 3v5e, 4emm, 4mxi - SaCLP – Staphylococcus aureus
- 3v5i, 4emp - SaCLP (mutant)
- 2zl0 - HpCLP – Helicobacter pylori
- 2zl3 - HpCLP (mutant)
- 4jcq, 4jct – LmCLP – Listeria monocytogenes
- 4jcr - LmCLP (mutant)
- CLP P subunit binary complex
- CLP A subunit
- CLP A subunit binary complex