› 2ktx

Solution NMR

COMPLETE KALIOTOXIN FROM ANDROCTONUS MAURETANICUS MAURETANICUS, NMR, 18 STRUCTURES

Released:
DOI: 10.2210/pdb2ktx/pdb
PDB entry 2ktx coloured by chain, ensemble of 18 models, front view.
PDB entry 2ktx coloured by chain, ensemble of 18 models, side view.
PDB entry 2ktx coloured by chain, ensemble of 18 models, top view.
Source organism: Androctonus mauritanicus mauritanicus
Primary publication:
3D structure of kaliotoxin: is residue 34 a key for channel selectivity?
Gair�� M, Romi R, Fern��ndez I, Rochat H, Martin-Eauclaire MF, Van Rietschoten J, Pons M, Giralt E
J. Pept. Sci. 3 314-9
PMID: 9262650

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-150266 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium channel toxin alpha-KTx 3.1 Chain: A
Molecule details ›
Chain: A
Length: 38 amino acids
Theoretical weight: 4.17 KDa
Source organism: Androctonus mauritanicus mauritanicus
Expression system: Not provided
UniProt:
  • Canonical: P24662 (Residues: 1-38; Coverage: 100%)
Sequence domains: Scorpion short toxin, BmKK2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY, SIMULATED ANNEALING
Expression system: Not provided

Quick links

Citations

3 review citations

Scorpion toxins specific for potassium (K+) channels: a historical overview of peptide bioengineering.
Bergeron et al. (2012)
2 more

5 mentions without citation

Chemical shift prediction for protein structure calculation and quality assessment using an optimally parameterized force field.
Nielsen et al. (2012)
4 more