› 1lt3

X-ray diffraction
2Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139158 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Heat-labile enterotoxin B chain Chains: D, E, F, G, H
Molecule details ›
Chains: D, E, F, G, H
Length: 103 amino acids
Theoretical weight: 11.81 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P32890 (Residues: 22-124; Coverage: 100%)
Gene names: eltB, ltpB
Sequence domains: Heat-labile enterotoxin beta chain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Heat-labile enterotoxin A chain Chain: A
Molecule details ›
Chain: A
Length: 240 amino acids
Theoretical weight: 27.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P06717 (Residues: 19-258; Coverage: 100%)
Gene names: eltA, ltpA
Sequence domains: Heat-labile enterotoxin alpha chain
Structure domains: Heat-Labile Enterotoxin, subunit A

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GAL
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 119.7Å b: 101.1Å c: 64.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.261
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Production of disulfide-bonded proteins in Escherichia coli.
Berkmen M. (2012)
1 more