2WVQ

Structure of the HET-s N-terminal domain. Mutant D23A, P33H

Summary for 2WVQ

Related2WVN 2WVO
DescriptorSMALL S PROTEIN, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, (2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL, ... (4 entities in total)
Functional Keywordsprion-binding protein, prion, prion regulatory domain, heterokaryon incompatibility, prion- binding protein
Biological sourcePODOSPORA ANSERINA
Total number of polymer chains2
Total molecular weight51222.43
Authors
Greenwald, J.,Buhtz, C.,Ritter, C.,Kwiatkowski, W.,Choe, S.,Saupe, S.J.,Riek, R. (deposition date: 2009-10-19, release date: 2010-07-28, Last modification date: 2019-02-27)
Primary citation
Greenwald, J.,Buhtz, C.,Ritter, C.,Kwiatkowski, W.,Choe, S.,Maddelein, M.L.,Ness, F.,Cescau, S.,Soragni, A.,Leitz, D.,Saupe, S.J.,Riek, R.
The mechanism of prion inhibition by HET-S.
Mol. Cell, 38:889-899, 2010
PubMed: 20620958 (PDB entries with the same primary citation)
DOI: 10.1016/j.molcel.2010.05.019
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.26690 15.6% 4.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload