› 2ktc

Solution NMR

Solution Structure of a Novel hKv1.1 inhibiting scorpion toxin from Mesibuthus tamulus

Released:
DOI: 10.2210/pdb2ktc/pdb
PDB entry 2ktc coloured by chain, ensemble of 20 models, front view.
PDB entry 2ktc coloured by chain, ensemble of 20 models, side view.
PDB entry 2ktc coloured by chain, ensemble of 20 models, top view.
Source organism: Mesobuthus tamulus
Primary publication:
Solution structure of BTK-2, a novel hK(v)1.1 inhibiting scorpion toxin, from the eastern Indian scorpion Mesobuthus tamulus.
Kumar GS, Upadhyay S, Mathew MK, Sarma SP
Biochim Biophys Acta 1814 459-69 (2011)
PMID: 21256986

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157980 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium channel toxin alpha-KTx 9.4 Chain: A
Molecule details ›
Chain: A
Length: 34 amino acids
Theoretical weight: 3.61 KDa
Source organism: Mesobuthus tamulus
Expression system: Escherichia coli
UniProt:
  • Canonical: P60209 (Residues: 1-32; Coverage: 100%)
Sequence domains: BmTXKS1/BmP02 toxin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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