1TYF

THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS

Summary for 1TYF

DescriptorCLP PEPTIDASE (2 entities in total)
Functional Keywordspeptidase
Biological sourceEscherichia coli
Cellular locationCytoplasm P0A6G7
Total number of polymer chains14
Total molecular weight302216.08
Authors
Wang, J.,Hartling, J.A.,Flanagan, J.M. (deposition date: 1997-10-13, release date: 1998-06-17, Last modification date: 2011-07-13)
Primary citation
Wang, J.,Hartling, J.A.,Flanagan, J.M.
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis.
Cell(Cambridge,Mass.), 91:447-456, 1997
PubMed: 9390554 (PDB entries with the same primary citation)
DOI: 10.1016/S0092-8674(00)80431-6
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.3 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.293182.1%8.5%3.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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