PDBe 3ofi

X-ray diffraction
2.35Å resolution

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

Released:
Source organism: Homo sapiens
Primary publication:
Ubiquitin is a novel substrate for human insulin-degrading enzyme.
J. Mol. Biol. 406 454-66 (2011)
PMID: 21185309

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 dimer (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: 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
Ubiquitin Chains: C, D
Molecule details ›
Chains: C, D
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family

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: 262.943Å b: 262.943Å c: 90.968Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.21 0.24
Expression system: Escherichia coli