3KTG

Structure of ClpP from Bacillus subtilis in monoclinic crystal form

Summary for 3KTG

Related3KTH 3KTI 3KTJ 3KTK
DescriptorATP-dependent Clp protease proteolytic subunit (2 entities in total)
Functional Keywordshydrolase, atp-binding, nucleotide-binding, protease, serine protease, stress response
Biological sourceBacillus subtilis
Cellular locationCytoplasm (By similarity) P80244
Total number of polymer chains7
Total molecular weight154302.89
Authors
Lee, B.-G.,Brotz-Oesterhelt, H.,Song, H.K. (deposition date: 2009-11-25, release date: 2010-03-23, Last modification date: 2011-07-13)
Primary citation
Lee, B.-G.,Park, E.Y.,Lee, K.-E.,Jeon, H.,Sung, K.H.,Paulsen, H.,Rubsamen-Schaeff, H.,Brotz-Oesterhelt, H.,Song, H.K.
Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism
Nat.Struct.Mol.Biol., 17:471-478, 2010
PubMed: 20305655 (PDB entries with the same primary citation)
DOI: 10.1038/nsmb.1787
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.4 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers140.1%4.9%5.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload