3e4a

X-ray diffraction
2.6Å resolution

Function and Biology Details

Reaction catalysed:
Degradation of insulin, glucagon and other polypeptides. No action on proteins.

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Insulin-degrading enzyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 1019 amino acids
Theoretical weight: 117.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14735 (Residues: 1-1019; Coverage: 100%)
Gene name: IDE
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like
HYDROXAMATE PEPTIDE II1 Chains: F, G
Molecule details ›
Chains: F, G
Length: 3 amino acids
Theoretical weight: 231 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P65
Unit cell:
a: 261.402Å b: 261.402Å c: 92.054Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.167 0.225
Expression systems:
  • Escherichia coli
  • Not provided