› 4re9

X-ray diffraction
2.91Å resolution

Function and Biology Details

Reaction catalysed: 
Degradation of insulin, glucagon and other polypeptides. No action on proteins.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147037 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: P14735 (Residues: 42-1019; Coverage: 96%)
Gene name: IDE
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like

Ligands and Environments

6 bound ligands:
Ligand ZN 2 x ZN
Ligand 3M9 2 x 3M9
Ligand EPE 2 x EPE
Ligand PEG 10 x PEG
Ligand 1PE 2 x 1PE
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P65
Unit cell:
a: 262.981Å b: 262.981Å c: 90.508Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.161 0.159 0.213
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Targeting Insulin-Degrading Enzyme to Treat Type 2 Diabetes Mellitus.
Tang WJ. (2016)
11 more

1 mention without citation

Catalytic site inhibition of insulin-degrading enzyme by a small molecule induces glucose intolerance in mice.
Deprez-Poulain et al. (2015)