› 2pta

Solution NMR

PANDINUS TOXIN K-A (PITX-KA) FROM PANDINUS IMPERATOR, NMR, 20 STRUCTURES

Released:
DOI: 10.2210/pdb2pta/pdb
PDB entry 2pta coloured by chain, ensemble of 20 models, front view.
PDB entry 2pta coloured by chain, ensemble of 20 models, side view.
PDB entry 2pta coloured by chain, ensemble of 20 models, top view.
Source organism: Pandinus imperator
Primary publication:
Solution structure for Pandinus toxin K-alpha (PiTX-K alpha), a selective blocker of A-type potassium channels.
Tenenholz TC, Rogowski RS, Collins JH, Blaustein MP, Weber DJ
Biochemistry 36 2763-71 (1997)
PMID: 9062103

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-157359 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium channel toxin alpha-KTx 7.1 Chain: A
Molecule details ›
Chain: A
Length: 35 amino acids
Theoretical weight: 4.05 KDa
Source organism: Pandinus imperator
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55927 (Residues: 13-47; Coverage: 100%)
Gene name: PTX-1
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: Escherichia coli BL21(DE3)

Quick links

Citations

11 citation in other articles

The 'functional' dyad of scorpion toxin Pi1 is not itself a prerequisite for toxin binding to the voltage-gated Kv1.2 potassium channels.
Mouhat et al. (2004)
10 more

3 mentions without citation

Computational simulations of interactions of scorpion toxins with the voltage-gated potassium ion channel.
Yu et al. (2004)
2 more