Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero heptamer (preferred)
Assembly name:
Heat-labile enterotoxin (preferred)
PDBe Complex ID:
PDB-CPX-139157 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Heat-labile enterotoxin B chain
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:
Sequence domains: Heat-labile enterotoxin beta chain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
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%)
Sequence domains: Heat-labile enterotoxin beta chain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Heat-labile enterotoxin A chain
Molecule details ›
Chain: A
Length: 192 amino acids
Theoretical weight: 22.09 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: Heat-labile enterotoxin alpha chain
Structure domains: Heat-Labile Enterotoxin, subunit A
Length: 192 amino acids
Theoretical weight: 22.09 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: P06717 (Residues: 19-210; Coverage: 80%)
Sequence domains: Heat-labile enterotoxin alpha chain
Structure domains: Heat-Labile Enterotoxin, subunit A
Heat-labile enterotoxin A chain
Molecule details ›
Chain: C
Length: 48 amino acids
Theoretical weight: 5.78 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 48 amino acids
Theoretical weight: 5.78 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: P06717 (Residues: 211-258; Coverage: 20%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
