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PDBe Entry: 1y7o 
The structure of Streptococcus pneumoniae A153P ClpP
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HYDROLASE
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X-RAY DIFFRACTION
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Resolution: 2.51 Å, R-factor: 19.222%, Free R-factor: 24.814%, Spacegroup: P 32 2 1
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08/02/2005, deposition: 09/12/2004, last revision: 24/02/2009
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Kimber, M.S.; Gribun, A.; Ching, R.; Sprangers, R.; Fiebig, K.M.; Houry, W.A.
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The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.
J.BIOL.CHEM. vol:280, pag:16185-16196 (2005) [PubMed ID 15701650 ]
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protease, HYDROLASE
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3.4.21.92 ExPASy BRENDA (A B C D E F G)
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Streptococcus pneumoniae 1313(A B C D E F G)
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ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (Endopeptidase Clp) P63788 (A B C D E F G)
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A, B, C, D, E, F, G
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| A, B, C, D, E, F, G |
ATP-dependent Clp protease proteolytic subunit |
Protein |
P63788 (CLPP_STRR6)
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218 |
81% |
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| A, C, F, B, G, E |
CALCIUM ION |
CA
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