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Solution NMR

SCORPION TOXIN BMTX1 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES

Released:
DOI: 10.2210/pdb1big/pdb
PDB entry 1big coloured by chain, ensemble of 25 models, front view.
PDB entry 1big coloured by chain, ensemble of 25 models, side view.
PDB entry 1big coloured by chain, ensemble of 25 models, top view.
Source organism: Mesobuthus martensii
Primary publication:
Solution structure of two new toxins from the venom of the Chinese scorpion Buthus martensi Karsch blockers of potassium channels.
Blanc E, Romi-Lebrun R, Bornet O, Nakajima T, Darbon H
Biochemistry 37 12412-8 (1998)
PMID: 9730813

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-192434 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium channel toxin alpha-KTx 1.5 Chain: A
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 4.18 KDa
Source organism: Mesobuthus martensii
Expression system: Not provided
UniProt:
  • Canonical: Q9NII6 (Residues: 21-57; 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
Refinement method: distance geometry
Expression system: Not provided

Quick links

Citations

5 review citations

An overview of toxins and genes from the venom of the Asian scorpion Buthus martensi Karsch.
Goudet et al. (2002)
4 more

2 mentions without citation

Optimal simultaneous superpositioning of multiple structures with missing data.
Theobald et al. (2012)
1 more