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Solution NMR

ANALYSIS OF SIDE-CHAIN ORGANIZATION ON A REFINED MODEL OF CHARYBDOTOXIN: STRUCTURAL AND FUNCTIONAL IMPLICATIONS

Released:
DOI: 10.2210/pdb2crd/pdb
PDB entry 2crd coloured by chain, ensemble of 12 models, front view.
PDB entry 2crd coloured by chain, ensemble of 12 models, side view.
PDB entry 2crd coloured by chain, ensemble of 12 models, top view.
Source organism: Leiurus quinquestriatus hebraeus
Primary publication:
Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications.
Bontems F, Gilquin B, Roumestand C, Ménez A, Toma F
Biochemistry 31 7756-64 (1992)
PMID: 1380828

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-146605 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium channel toxin alpha-KTx 1.1 Chain: A
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 4.31 KDa
Source organism: Leiurus quinquestriatus hebraeus
Expression system: Not provided
UniProt:
  • Canonical: P13487 (Residues: 23-59; Coverage: 100%)
Sequence domains: Scorpion short toxin, BmKK2

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

13 review citations

High-conductance calcium-activated potassium channels; structure, pharmacology, and function.
Kaczorowski et al. (1996)
12 more

37 mentions without citation

Sea anemone (Cnidaria, Anthozoa, Actiniaria) toxins: an overview.
Frazão et al. (2012)
36 more