2be1

X-ray diffraction
2.98Å resolution

Structure of the compact lumenal domain of yeast Ire1

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
On the mechanism of sensing unfolded protein in the endoplasmic reticulum.
Proc Natl Acad Sci U S A 102 18773-84 (2005)
PMID: 16365312

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-152279 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase/endoribonuclease IRE1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 339 amino acids
Theoretical weight: 38.13 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P32361 (Residues: 111-449; Coverage: 31%)
Gene names: ERN1, IRE1, YHR079C
peptide Chain: D
Molecule details ›
Chain: D
Length: 8 amino acids
Theoretical weight: 811 Da
Source organism: Saccharomyces cerevisiae
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P6522
Unit cell:
a: 103.3Å b: 103.3Å c: 401.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.24 0.279
Expression systems:
  • Escherichia coli
  • Not provided