The ab initio structure determination and refinement of a scorpion protein toxin. Determined by X-ray diffraction at 0.96 Å resolution. Released 15 Oct 1997.
Explore 1AHO in 3D Show helices and sheets RCSB PDB PDBe
1AHO contains 1 α-helix and 7 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-5 | 4 | 1 |
| β-strand | 6 | 1 | 2 |
| β-strand | 7 | 1 | 3 |
| β-strand | 13 | 1 | 3 |
| α-helix | 19-28 | 10 | |
| β-strand | 33-41 | 9 | 1 |
| β-strand | 43-51 | 9 | 1 |
| β-strand | 57 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Toxin II | A | protein | 64 | Androctonus australis | P01484 (AlphaFold model) |
>1AHO_1 TOXIN II (chains A) VKDGYIVDDVNCTYFCGRNAYCNEECTKLKGESGYCQWASPYGNACYCYKLPDHVRTKGP GRCH
Ab initio structure determination and refinement of a scorpion protein toxin. Smith, G.D., Blessing, R.H., Ealick, S.E. et al. Acta Crystallogr D Biol Crystallogr (1997) 53:551-557. DOI 10.1107/S0907444997005386 · PubMed
Other PDB entries of the same protein (UniProt P01484 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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