5NVR

Crystal structure of the Rif1 N-terminal domain (RIF1-NTD) from Saccharomyces cerevisiae

Summary for 5NVR

DescriptorTelomere length regulator protein RIF1 (1 entity in total)
Functional Keywordstelomere maintenance, dna double-strand break repair, irregular helical repeat, all-alpha fold, structural protein
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Total number of polymer chains1
Total molecular weight129054.05
Authors
Bunker, R.D.,Shi, T.,Thoma, N.H. (deposition date: 2017-05-04, release date: 2017-06-14, Last modification date: 2019-04-03)
Primary citation
Mattarocci, S.,Reinert, J.K.,Bunker, R.D.,Fontana, G.A.,Shi, T.,Klein, D.,Cavadini, S.,Faty, M.,Shyian, M.,Hafner, L.,Shore, D.,Thoma, N.H.,Rass, U.
Rif1 maintains telomeres and mediates DNA repair by encasing DNA ends.
Nat. Struct. Mol. Biol., 24:588-595, 2017
PubMed: 28604726 (PDB entries with the same primary citation)
DOI: 10.1038/nsmb.3420
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (3.95 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.2632 1.6% 3.0% 6.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
171588
PDB entries from 2020-11-25