› 1etl

X-ray diffraction
0.89Å resolution

STRUCTURAL CHARACTERISTICS FOR BIOLOGICAL ACTIVITY OF HEAT-STABLE ENTEROTOXIN PRODUCED BY ENTEROTOXIGENIC ESCHERICHIA COLI: X-RAY CRYSTALLOGRAPHY OF WEAKLY TOXIC AND NONTOXIC ANALOGS

Released:
DOI: 10.2210/pdb1etl/pdb
PDB entry 1etl coloured by chain, front view.
PDB entry 1etl coloured by chain, side view.
PDB entry 1etl coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural characteristics for biological activity of heat-stable enterotoxin produced by enterotoxigenic Escherichia coli: X-ray crystallography of weakly toxic and nontoxic analogs.
Sato T, Ozaki H, Hata Y, Kitagawa Y, Katsube Y, Shimonishi Y
Biochemistry 33 8641-50 (1994)
PMID: 8038153

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134389 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat-stable enterotoxin ST-IA/ST-P Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.24 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P01559 (Residues: 60-71; Coverage: 23%)
Gene name: sta1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 21.928Å b: 10.219Å c: 17.891Å
α: 90° β: 111.71° γ: 90°
R-values:
R R work R free
0.073 0.073 not available
Expression system: Not provided

Quick links

Citations

7 review citations

Enteric bacterial toxins: mechanisms of action and linkage to intestinal secretion.
Sears et al. (1996)
6 more

11 mentions without citation

PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides.
Thévenet et al. (2012)
10 more