› 2mvt

Solution NMR

Solution structure of scoloptoxin SSD609 from Scolopendra mutilans

Released:
DOI: 10.2210/pdb2mvt/pdb
PDB entry 2mvt coloured by chain, ensemble of 20 models, front view.
PDB entry 2mvt coloured by chain, ensemble of 20 models, side view.
PDB entry 2mvt coloured by chain, ensemble of 20 models, top view.
Source organism: Scolopendra subspinipes
Primary publication:
A distinct three-helix centipede toxin SSD609 inhibits I(ks) channels by interacting with the KCNE1 auxiliary subunit.
Sun P, Wu F, Wen M, Yang X, Wang C, Li Y, He S, Zhang L, Zhang Y, Tian C
OpenAccess logo Sci Rep 5 13399 (2015)
PMID: 26307551

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102614 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kappa-scoloptoxin(03)-Ssd1a Chain: A
Molecule details ›
Chain: A
Length: 47 amino acids
Theoretical weight: 5.64 KDa
Source organism: Scolopendra subspinipes
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0R4I951 (Residues: 24-70; Coverage: 100%)
Structure domains: Diphtheria Toxin Repressor; domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 39%
Refinement method: simulated annealing
Expression system: Escherichia coli

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Citations

3 review citations

Animal toxins - Nature's evolutionary-refined toolkit for basic research and drug discovery.
Herzig et al. (2020)
2 more

3 mentions without citation

Centipede Venom Peptides Acting on Ion Channels.
Chu et al. (2020)
2 more