2rio

X-ray diffraction
2.4Å resolution

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

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-152278 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase/endoribonuclease IRE1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 434 amino acids
Theoretical weight: 50.04 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P32361 (Residues: 658-1115; Coverage: 40%)
Gene names: ERN1, IRE1, YHR079C
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P65
Unit cell:
a: 130.307Å b: 130.307Å c: 175.011Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.222 0.266
Expression system: Escherichia coli BL21