2RIO
Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing
Summary for 2RIO
Entry DOI | 10.2210/pdb2rio/pdb |
Descriptor | Serine/threonine-protein kinase/endoribonuclease IRE1, MAGNESIUM ION, STRONTIUM ION, ... (4 entities in total) |
Functional Keywords | protein-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 source | Saccharomyces cerevisiae (baker's yeast) More |
Cellular location | Endoplasmic reticulum membrane; Single-pass type I membrane protein: P32361 |
Total number of polymer chains | 2 |
Total formula weight | 101155.05 |
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: 2024-02-21) |
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 Cited by PubMed: 18191223DOI: 10.1016/j.cell.2007.10.057 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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