PDBe 2wby

X-ray diffraction
2.6Å resolution

Crystal structure of human insulin-degrading enzyme in complex with insulin

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
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 BL21(DE3)
UniProt:
  • Canonical: P14735 (Residues: 42-1019; Coverage: 96%)
Gene name: IDE
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like
Insulin A chain Chains: C, E
Molecule details ›
Chains: C, E
Length: 20 amino acids
Theoretical weight: 2.27 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01308 (Residues: 90-109; Coverage: 23%)
Gene name: INS
Insulin B chain Chains: D, F
Molecule details ›
Chains: D, F
Length: 19 amino acids
Theoretical weight: 2.15 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01308 (Residues: 25-43; Coverage: 22%)
Gene name: INS

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P65
Unit cell:
a: 262.319Å b: 262.319Å c: 90.609Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.164 0.218
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided