5uoe

X-ray diffraction
3.8Å resolution

Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (IDE)

Released:
Source organism: Homo sapiens
Entry authors: Liang WG, Bailey L, Kossiakoff T, Tang WJ

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Insulin-degrading enzyme Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
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: Metalloenzyme, LuxS/M16 peptidase-like
FAB Heavy chain with engineered elbow Chains: H, M, P, S, V
Molecule details ›
Chains: H, M, P, S, V
Length: 229 amino acids
Theoretical weight: 24.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
FAB light chain Chains: L, N, Q, T, W
Molecule details ›
Chains: L, N, Q, T, W
Length: 215 amino acids
Theoretical weight: 23.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 18-ID
Unit cell:
a: 131.321Å b: 242.048Å c: 310.757Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.22 0.27
Expression system: Escherichia coli