PDBe 3p7o

X-ray diffraction
2.14Å resolution

Rat Insulin Degrading Enzyme (Insulysin) E111F mutant with two bound peptides

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

Assemblies composition:
hetero hexamer
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Insulin-degrading enzyme Chain: A
Molecule details ›
Chain: A
Length: 1019 amino acids
Theoretical weight: 117.88 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P35559 (Residues: 1-1019; Coverage: 100%)
Gene name: Ide
Sequence domains:
Structure domains: Cytochrome Bc1 Complex; Chain A, domain 1
active site bound peptide Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 699 Da
Source organism: Rattus norvegicus
Expression system: Escherichia coli
distal site bound peptide Chain: C
Molecule details ›
Chain: C
Length: 7 amino acids
Theoretical weight: 614 Da
Source organism: Rattus norvegicus
Expression system: Escherichia coli

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 115.52Å b: 70.91Å c: 114.36Å
α: 90° β: 92.97° γ: 90°
R-values:
R R work R free
0.221 0.208 0.285
Expression system: Escherichia coli