Contact-dependent inhibition system from Escherichia coli NC101 - ternary CdiA/CdiI/EF-Tu complex (trypsin-modified)

Summary for 5I4R

DescriptorContact-dependent inhibitor A, Elongation factor Tu, Contact-dependent inhibitor I, ... (5 entities in total)
Functional Keywordstoxin, antitoxin, elongation factor, structural genomics, psi-biology, midwest center for structural genomics, mcsg, structure-function analysis of polymorphic cdi toxin-immunity protein complexes, uc4cdi, toxin-antitoxin complex, toxin/antitoxin
Biological sourceEscherichia coli NC101
Total number of polymer chains8
Total molecular weight133836.14
Primary citation
Michalska, K.,Gucinski, G.C.,Garza-Sanchez, F.,Johnson, P.M.,Stols, L.M.,Eschenfeldt, W.H.,Babnigg, G.,Low, D.A.,Goulding, C.W.,Joachimiak, A.,Hayes, C.S.
Structure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific transfer RNAs.
Nucleic Acids Res., 45:10306-10320, 2017
PubMed: 28973472 (PDB entries with the same primary citation)
DOI: 10.1093/nar/gkx700
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.267400.4%1.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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PDB entries from 2020-09-16