NMR structures of lqh III alpha-like scorpion toxin from leiurus quinquestriatus corresponding to the major conformer in solution. Determined by solution NMR. Released 23 Aug 2000.
Explore 1FH3 in 3D Show helices and sheets RCSB PDB PDBe
1FH3 contains 1 α-helix and 4 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 | 2-6 | 5 | 1 |
| α-helix | 21-30 | 10 | |
| β-strand | 34-40 | 7 | 1 |
| β-strand | 44-52 | 9 | 1 |
| β-strand | 58 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lqh III alpha-like toxin | A | protein | 68 | Leiurus quinquestriatus hebraeus | P56678 (AlphaFold model) |
>1FH3_1 LQH III ALPHA-LIKE TOXIN (chains A) VRDGYIAQPENCVYHCFPGSSGCDTLCKEKGGTSGHCGFKVGHGLACWCNALPDNVGIIV EGEKCHSX
A Cis-trans Isomerism of a Non-prolyl Peptide Bond in Lqh III Alpha-like Scorpion Toxin Revealed by Solution NMR. Krimm, I., Trivelli, X., Lancelin, J.M. To be published.
Other PDB entries of the same protein (UniProt P56678 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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