A two disulfide derivative of charybdotoxin with disulfide 13-33 replaced by two alpha-aminobutyric acids, NMR, 30 structures. Determined by solution NMR. Released 11 Jan 1997.
Explore 1BAH in 3D Show helices and sheets RCSB PDB PDBe
1BAH contains 1 α-helix and 2 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 |
|---|---|---|---|
| α-helix | 16-20 | 5 | |
| β-strand | 28 | 1 | 1 |
| β-strand | 33 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Charybdotoxin | A | protein | 37 | Leiurus quinquestriatus | P13487 (AlphaFold model) |
>1BAH_1 CHARYBDOTOXIN (chains A) QFTNVSCTTSKEAWSVCQRLHNTSRGKCMNKKARCYS
NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing. Song, J., Gilquin, B., Jamin, N. et al. Biochemistry (1997) 36:3760-3766. DOI 10.1021/bi962720h · PubMed
Other PDB entries of the same protein (UniProt P13487 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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