› 2jbu

X-ray diffraction
3Å resolution

Crystal structure of human insulin degrading enzyme complexed with co- purified peptides.

Released:
DOI: 10.2210/pdb2jbu/pdb
PDB entry 2jbu coloured by chain, front view.
PDB entry 2jbu coloured by chain, side view.
PDB entry 2jbu coloured by chain, top view.
Source organisms:
Primary publication:
Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE.
Im H, Manolopoulou M, Malito E, Shen Y, Zhao J, Neant-Fery M, Sun CY, Meredith SC, Sisodia SS, Leissring MA, Tang WJ
J Biol Chem 282 25453-63 (2007)
PMID: 17613531

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147039 (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: 114.72 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
CO-PURIFIED PEPTIDE Chains: C, D
Molecule details ›
Chains: C, D
Length: 12 amino acids
Theoretical weight: 871 Da
Source organism: Escherichia coli
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand DIO 2 x DIO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P65
Unit cell:
a: 263.277Å b: 263.277Å c: 90.735Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.186 0.24
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli

Quick links

Citations

18 review citations

European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS).
Egea et al. (2017)
17 more

2 mentions without citation

Comparative Study of Two Insulinlike Proteases in Cryptosporidium parvum.
He et al. (2021)
1 more