Structure of a viral OTU domain protease bound to Ubiquitin

Summary for 3PT2

DescriptorRNA polymerase, Ubiquitin B, SULFATE ION, ... (6 entities in total)
Functional Keywordsviral deubiquitinase, 3-aminopropane, intein-mediated ligation, isg15, crimean-congo hemorrhagic fever virus, hydrolase-protein binding complex, hydrolase/protein binding
Biological sourceCrimean-Congo hemorrhagic fever virus
Total number of polymer chains2
Total molecular weight30363.21
James, T.W.,Bacik, J.P.,Frias-Staheli, N.,Garcia-Sastre, A.,Mark, B.L. (deposition date: 2010-12-02, release date: 2011-01-19, Last modification date: 2017-11-08)
Primary citation
James, T.W.,Frias-Staheli, N.,Bacik, J.P.,Levingston Macleod, J.M.,Khajehpour, M.,Garcia-Sastre, A.,Mark, B.L.
Structural basis for the removal of ubiquitin and interferon-stimulated gene 15 by a viral ovarian tumor domain-containing protease.
Proc.Natl.Acad.Sci.USA, 108:2222-2227, 2011
PubMed: 21245344 (PDB entries with the same primary citation)
DOI: 10.1073/pnas.1013388108
MImport into Mendeley
Experimental method
NMR Information

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.219501.4%0.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report