PDBe 4m1c

X-ray diffraction
3.5Å resolution

Crystal Structure Analysis of Fab-Bound Human Insulin Degrading Enzyme (IDE) in Complex with Amyloid-Beta (1-40)

Released:
Source organism: Homo sapiens
Entry authors: McCord LM, Liang W, Farcasanu M, Scherpelz K, Meredith SC, Koide S, Tang WJ

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Beta-amyloid protein 40 Chains: G, H
Molecule details ›
Chains: G, H
Length: 40 amino acids
Theoretical weight: 4.34 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 672-711; Coverage: 5%)
Gene names: A4, AD1, APP
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
UniProt:
  • Canonical: P14735 (Residues: 42-1019; Coverage: 96%)
Gene name: IDE
Sequence domains:
Structure domains: Cytochrome Bc1 Complex; Chain A, domain 1
Fab-bound IDE, heavy chain Chains: C, E
Molecule details ›
Chains: C, E
Length: 263 amino acids
Theoretical weight: 28.2 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Structure domains: Immunoglobulins
Fab-bound IDE, light chain Chains: D, F
Molecule details ›
Chains: D, F
Length: 239 amino acids
Theoretical weight: 25.98 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 56.583Å b: 135.324Å c: 368.524Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.228 0.27
Expression systems:
  • Not provided
  • Escherichia coli