› 1lqq

Solution NMR

ANTI-MAMMAL AND ANTI-INSECT LQQIII SCORPION TOXIN, NMR, 15 STRUCTURES

Released:
DOI: 10.2210/pdb1lqq/pdb
PDB entry 1lqq coloured by chain, ensemble of 15 models, front view.
PDB entry 1lqq coloured by chain, ensemble of 15 models, side view.
PDB entry 1lqq coloured by chain, ensemble of 15 models, top view.
Source organism: Leiurus quinquestriatus quinquestriatus
Primary publication:
1H-NMR-derived secondary structure and the overall fold of the potent anti-mammal and anti-insect toxin III from the scorpion Leiurus quinquestriatus quinquestriatus.
Landon C, Cornet B, Bonmatin JM, Kopeyan C, Rochat H, Vovelle F, Ptak M
Eur J Biochem 236 395-404 (1996)
PMID: 8612608

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-insect toxin Lqq3 Chain: A
Molecule details ›
Chain: A
Length: 64 amino acids
Theoretical weight: 7.25 KDa
Source organism: Leiurus quinquestriatus quinquestriatus
UniProt:
  • Canonical: P01487 (Residues: 1-64; Coverage: 100%)
Sequence domains: Scorpion toxin-like domain
Structure domains: Knottin, scorpion toxin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing

Quick links

Citations

1 review citation

Properties of cytotoxic peptide-formed ion channels.
Kourie et al. (2000)
19 other articles

5 mentions without citation

A new type of scorpion Na+-channel-toxin-like polypeptide active on K+ channels.
Srairi-Abid et al. (2005)
4 more