3fbv

X-ray diffraction
3.2Å resolution

Crystal structure of the oligomer formed by the kinase-ribonuclease domain of Ire1

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetradecamer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase/endoribonuclease IRE1 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 448 amino acids
Theoretical weight: 51.88 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P32361 (Residues: 641-1115; Coverage: 41%)
Gene names: ERN1, IRE1, YHR079C
Sequence domains: Ribonuclease 2-5A
Structure domains:

Ligands and Environments

1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21212
Unit cell:
a: 156.82Å b: 163.47Å c: 292.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.235 0.284
Expression system: Escherichia coli