3cww

X-ray diffraction
1.96Å resolution

Crystal Structure of IDE-bradykinin complex

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-147046 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Insulin-degrading enzyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 990 amino acids
Theoretical weight: 113.89 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
bradykinin N-terminal tetrapeptide analogue Chains: D, E
Molecule details ›
Chains: D, E
Length: 4 amino acids
Theoretical weight: 354 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P65
Unit cell:
a: 262.448Å b: 262.448Å c: 90.628Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.181 0.208
Expression systems:
  • Escherichia coli
  • Not provided