3n56

X-ray diffraction
3.1Å resolution

Crystal Structure of human Insulin-degrading enzyme (IDE) in complex with human B-type natriuretic peptide (BNP)

Released:
Source organism: Homo sapiens
Entry authors: Funke T, Guo Q, Tang W-J

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-147038 (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 BL21(DE3)
UniProt:
  • Canonical: P14735 (Residues: 42-1019; Coverage: 96%)
Gene name: IDE
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like
Brain natriuretic peptide 32 Chains: C, D
Molecule details ›
Chains: C, D
Length: 32 amino acids
Theoretical weight: 3.47 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P16860 (Residues: 103-134; Coverage: 30%)
Gene name: NPPB
Sequence domains: Atrial natriuretic peptide

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: 264.036Å b: 264.036Å c: 90.645Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.202 0.243
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided