2RIO

Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing

Summary for 2RIO

DescriptorSerine/threonine-protein kinase/endoribonuclease IRE1, MAGNESIUM ION, STRONTIUM ION, ... (4 entities in total)
Functional Keywordsprotein-nucleotide complex, atp-binding, endoplasmic reticulum, glycoprotein, hydrolase, kinase, magnesium, membrane, metal-binding, multifunctional enzyme, nucleotide-binding, phosphorylation, serine/threonine-protein kinase, transcription, transcription regulation, transferase, transmembrane, unfolded protein response
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationEndoplasmic reticulum membrane; Single-pass type I membrane protein P32361
Total number of polymer chains2
Total molecular weight101155.05
Authors
Lee, K.P.,Dey, M.,Neculai, D.,Cao, C.,Dever, T.E.,Sicheri, F. (deposition date: 2007-10-12, release date: 2008-01-29, Last modification date: 2017-08-09)
Primary citation
Lee, K.P.,Dey, M.,Neculai, D.,Cao, C.,Dever, T.E.,Sicheri, F.
Structure of the dual enzyme ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing.
Cell(Cambridge,Mass.), 132:89-100, 2008
PubMed: 18191223 (PDB entries with the same primary citation)
DOI: 10.1016/j.cell.2007.10.057
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.4 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.266151.9%12.0%2.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution