Actin dimer cross-linked by V. cholerae MARTX toxin and complexed with DNase I and Gelsolin-segment 1

Summary for 3CJC

DescriptorActin, alpha skeletal muscle, Deoxyribonuclease-1, Gelsolin, ... (8 entities in total)
Functional Keywordscross-linked dimer, atp-binding, cytoskeleton, methylation, muscle protein, nucleotide-binding, phosphoprotein, structural protein, actin-binding, apoptosis, endonuclease, glycoprotein, hydrolase, nuclease, nucleus, secreted, actin capping, alternative initiation, amyloid, disease mutation, structural protein-hydrolase complex, structural protein/hydrolase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm, cytoskeleton P68135
Secreted P00639
Isoform 2: Cytoplasm, cytoskeleton. Isoform 1: Secreted P06396
Total number of polymer chains3
Total molecular weight86867.49
Sawaya, M.R.,Kudryashov, D.S.,Pashkov, I.,Reisler, E.,Yeates, T.O. (deposition date: 2008-03-12, release date: 2008-03-25, Last modification date: 2017-10-25)
Primary citation
Kudryashov, D.S.,Durer, Z.A.,Ytterberg, A.J.,Sawaya, M.R.,Pashkov, I.,Prochazkova, K.,Yeates, T.O.,Loo, R.R.,Loo, J.A.,Satchell, K.J.,Reisler, E.
Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin.
Proc.Natl.Acad.Sci.USA, 105:18537-18542, 2008
PubMed: 19015515 (PDB entries with the same primary citation)
DOI: 10.1073/pnas.0808082105
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.295110.1%2.9%3.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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