PDBe 6b70

Electron Microscopy
3.7Å resolution

Cryo-EM structure of human insulin degrading enzyme in complex with FAB H11-E heavy chain, FAB H11-E light chain and 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 tetramer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Insulin-degrading enzyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 966 amino acids
Theoretical weight: 111.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14735 (Residues: 46-1011; Coverage: 95%)
Gene name: IDE
Sequence domains:
FAB H11-E heavy chain Chains: C, E
Molecule details ›
Chains: C, E
Length: 218 amino acids
Theoretical weight: 23.06 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
FAB H11-E light chain Chains: D, F
Molecule details ›
Chains: D, F
Length: 211 amino acids
Theoretical weight: 23.09 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
Insulin Chains: a, c
Molecule details ›
Chains: a, c
Length: 110 amino acids
Theoretical weight: 11.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01308 (Residues: 1-110; Coverage: 100%)
Gene name: INS
Sequence domains: Insulin/IGF/Relaxin family

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.7Å
Relevant EMDB volumes: EMD-7062
Expression system: Escherichia coli