› 1bgk

Solution NMR

SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES

Released:
DOI: 10.2210/pdb1bgk/pdb
PDB entry 1bgk coloured by chain, ensemble of 15 models, front view.
PDB entry 1bgk coloured by chain, ensemble of 15 models, side view.
PDB entry 1bgk coloured by chain, ensemble of 15 models, top view.
Source organism: Bunodosoma granuliferum
Primary publication:
On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures.
Dauplais M, Lecoq A, Song J, Cotton J, Jamin N, Gilquin B, Roumestand C, Vita C, de Medeiros CL, Rowan EG, Harvey AL, Ménez A
J Biol Chem 272 4302-9 (1997)
PMID: 9020148

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151363 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kappa-actitoxin-Bgr1a Chain: A
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 4.29 KDa
Source organism: Bunodosoma granuliferum
Expression system: Not provided
UniProt:
  • Canonical: P29186 (Residues: 1-37; Coverage: 100%)
Sequence domains: ShK domain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

37 review citations

Conus venoms: a rich source of novel ion channel-targeted peptides.
Terlau et al. (2004)
36 more

15 mentions without citation

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