› 1du9

Solution NMR

SOLUTION STRUCTURE OF BMP02, A NATURAL SCORPION TOXIN WHICH BLOCKS APAMIN-SENSITIVE CALCIUM-ACTIVATED POTASSIUM CHANNELS, 25 STRUCTURES

Released:
DOI: 10.2210/pdb1du9/pdb
PDB entry 1du9 coloured by chain, ensemble of 25 models, front view.
PDB entry 1du9 coloured by chain, ensemble of 25 models, side view.
PDB entry 1du9 coloured by chain, ensemble of 25 models, top view.
Source organism: Mesobuthus martensii
Primary publication:
Solution structure of BmP02, a new potassium channel blocker from the venom of the Chinese scorpion Buthus martensi Karsch.
Xu Y, Wu J, Pei J, Shi Y, Ji Y, Tong Q
Biochemistry 39 13669-75 (2000)
PMID: 11076505

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-192438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium channel toxin alpha-KTx 9.1 Chain: A
Molecule details ›
Chain: A
Length: 28 amino acids
Theoretical weight: 2.96 KDa
Source organism: Mesobuthus martensii
UniProt:
  • Canonical: Q9NJP7 (Residues: 29-56; Coverage: 100%)
Sequence domains: BmTXKS1/BmP02 toxin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Refinement method: simulated annealing and ENERGY MINIMIZATION

Quick links

Citations

1 review citation

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

7 mentions without citation

Kv1.3 Channel as a Key Therapeutic Target for Neuroinflammatory Diseases: State of the Art and Beyond.
Wang et al. (2019)
6 more