› 1bah

Solution NMR

A TWO DISULFIDE DERIVATIVE OF CHARYBDOTOXIN WITH DISULFIDE 13-33 REPLACED BY TWO ALPHA-AMINOBUTYRIC ACIDS, NMR, 30 STRUCTURES

Released:
DOI: 10.2210/pdb1bah/pdb
PDB 1bah coloured by chain and viewed from the front.
PDB 1bah coloured by chain and viewed from the side.
PDB 1bah coloured by chain and viewed from the top.
Source organism: Leiurus quinquestriatus
Primary publication:
NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing.
Song J, Gilquin B, Jamin N, Drakopoulou E, Guenneugues M, Dauplais M, Vita C, Ménez A
Biochemistry 36 3760-6 (1997)
PMID: 9092804

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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: 4.27 KDa
Source organism: Leiurus quinquestriatus
Expression system: Not provided
UniProt:
  • Canonical: P13487 (Residues: 23-59; Coverage: 100%)
Sequence domains: Scorpion short toxin, BmKK2

Ligands and Environments

No bound ligands
2 modified residues:
Ligand PCA 1 x PCA
Ligand ABA 2 x ABA

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

4 review citations

Incorporation of post-translational modified amino acids as an approach to increase both chemical and biological diversity of conotoxins and conopeptides.
Espiritu et al. (2014)
3 more

1 mention without citation

The Kunitz-Type Protein ShPI-1 Inhibits Serine Proteases and Voltage-Gated Potassium Channels.
García-Fernández et al. (2016)