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Solution NMR

DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF MARGATOXIN BY 1H, 13C, 15N TRIPLE-RESONANCE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Released:
DOI: 10.2210/pdb1mtx/pdb
PDB entry 1mtx coloured by chain, ensemble of 23 models, front view.
PDB entry 1mtx coloured by chain, ensemble of 23 models, side view.
PDB entry 1mtx coloured by chain, ensemble of 23 models, top view.
Source organism: Centruroides margaritatus
Primary publication:
Determination of the three-dimensional structure of margatoxin by 1H, 13C, 15N triple-resonance nuclear magnetic resonance spectroscopy.
Johnson BA, Stevens SP, Williamson JM
Biochemistry 33 15061-70 (1994)
PMID: 7999764

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-154180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium channel toxin alpha-KTx 2.2 Chain: A
Molecule details ›
Chain: A
Length: 39 amino acids
Theoretical weight: 4.19 KDa
Source organism: Centruroides margaritatus
UniProt:
  • Canonical: P40755 (Residues: 1-39; Coverage: 100%)
Sequence domains: Scorpion short toxin, BmKK2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores

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Citations

7 review citations

Therapeutic potential of venom peptides.
Lewis et al. (2003)
6 more

10 mentions without citation

Computational methods of studying the binding of toxins from venomous animals to biological ion channels: theory and applications.
Gordon et al. (2013)
9 more