X-ray diffraction
3.2Å resolution

Crystal structure of human insulin degrading enzyme (ide) in complex with inhibitor N-benzyl-N-(carboxymethyl)glycyl-L-histidine


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Insulin-degrading enzyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 990 amino acids
Theoretical weight: 114.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P14735 (Residues: 42-1019; Coverage: 96%)
Gene name: IDE
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P65
Unit cell:
a: 264.505Å b: 264.505Å c: 90.543Å
α: 90° β: 90° γ: 120°
R R work R free
0.18 0.179 0.222
Expression system: Escherichia coli