› 1hp3

Solution NMR

C-TERMINAL TRUNCATION OF OMEGA-ATRACOTOXIN-HV2A (CT-HV2A)

Released:
DOI: 10.2210/pdb1hp3/pdb
PDB entry 1hp3 coloured by chain, ensemble of 20 models, front view.
PDB entry 1hp3 coloured by chain, ensemble of 20 models, side view.
PDB entry 1hp3 coloured by chain, ensemble of 20 models, top view.
Source organism: Hadronyche versuta
Primary publication:
Discovery and structure of a potent and highly specific blocker of insect calcium channels.
Wang XH, Connor M, Wilson D, Wilson HI, Nicholson GM, Smith R, Shaw D, Mackay JP, Alewood PF, Christie MJ, King GF
J Biol Chem 276 40306-12 (2001)
PMID: 11522785

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160646 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Omega-hexatoxin-Hv2a Chain: A
Molecule details ›
Chain: A
Length: 32 amino acids
Theoretical weight: 3.38 KDa
Source organism: Hadronyche versuta
Expression system: Not provided
UniProt:
  • Canonical: P82852 (Residues: 1-32; Coverage: 71%)
Sequence domains: Magi 5 toxic peptide family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Torsion angle dynamics followed by dynamical simulated annealing
Expression system: Not provided

Quick links

Citations

16 review citations

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