› 1b44

X-ray diffraction
3.3Å resolution

CRYSTAL STRUCTURE OF THE B SUBUNIT OF HEAT-LABILE ENTEROTOXIN FROM E. COLI CARRYING A PEPTIDE WITH ANTI-HSV ACTIVITY

Released:
DOI: 10.2210/pdb1b44/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1b44 coloured by chain, front view.
PDB entry 1b44 coloured by chain, side view.
PDB entry 1b44 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the B subunit of Escherichia coli heat-labile enterotoxin carrying peptides with anti-herpes simplex virus type 1 activity.
Matković-Calogović D, Loregian A, D'Acunto MR, Battistutta R, Tossi A, Palù G, Zanotti G
J Biol Chem 274 8764-9 (1999)
PMID: 10085117

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143523 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat-labile enterotoxin B chain Chains: D, E, F, G, H
Molecule details ›
Chains: D, E, F, G, H
Length: 129 amino acids
Theoretical weight: 14.29 KDa
Source organism: Escherichia coli
Expression system: Vibrio cholerae
UniProt:
  • Canonical: P0CK94 (Residues: 22-124; Coverage: 100%)
Gene names: eltB, ltpB
Sequence domains: Heat-labile enterotoxin beta chain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P41212
Unit cell:
a: 127.1Å b: 127.1Å c: 176.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.255
Expression system: Vibrio cholerae

Quick links

Citations

3 review citations

Protein-protein interactions as targets for antiviral chemotherapy.
Loregian et al. (2002)
2 more

2 mentions without citation

Structural bioinformatic analysis of DsbA proteins and their pathogenicity associated substrates.
Santos-Martin et al. (2021)
1 more