PDBe 5wob

X-ray diffraction
3.95Å resolution

Crystal Structure Analysis of Fab1-Bound Human Insulin Degrading Enzyme (IDE) in Complex with Insulin

Released:
Source organisms:
Entry authors: McCord LA, Liang WG, Farcasanu M, Wang AG, Koide S, Tang WJ

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 octamer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Insulin-degrading enzyme Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
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:
Insulin A chain Chains: a, b, c, d, e, f, g, h
Molecule details ›
Chains: a, b, c, d, e, f, g, h
Length: 20 amino acids
Theoretical weight: 2.27 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P01308 (Residues: 90-109; Coverage: 23%)
Gene name: INS
IDE-bound Fab heavy chain Chains: I, K, M, O, Q, S, U, W
Molecule details ›
Chains: I, K, M, O, Q, S, U, W
Length: 263 amino acids
Theoretical weight: 28.2 KDa
Source organism: Mus musculoides
Expression system: Escherichia coli
IDE-bound Fab light chain Chains: J, L, N, P, R, T, V, X
Molecule details ›
Chains: J, L, N, P, R, T, V, X
Length: 239 amino acids
Theoretical weight: 25.98 KDa
Source organism: Mus musculoides
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 121.589Å b: 138.19Å c: 376.509Å
α: 90° β: 99.36° γ: 90°
R-values:
R R work R free
0.244 0.243 0.291
Expression systems:
  • Escherichia coli
  • Saccharomyces cerevisiae