3n57

X-ray diffraction
3.03Å resolution

Crystal Structure of human Insulin-degrading enzyme (IDE) in complex with human atrial natriuretic peptide (ANP)

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 tetramer (preferred)
PDBe Complex ID:
PDB-CPX-134082 (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
Atrial natriuretic peptide Chains: C, D
Molecule details ›
Chains: C, D
Length: 28 amino acids
Theoretical weight: 3.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01160 (Residues: 124-151; Coverage: 22%)
Gene names: ANP, NPPA, PND
Sequence domains: Atrial natriuretic peptide

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P65
Unit cell:
a: 264.101Å b: 264.101Å c: 91.186Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.206 0.242
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli