NMR solution structure of a chimeric protein, designed by transferring a functional snake beta-hairpin into a scorpion alpha/beta scaffold (PH 3.5, 20C), NMR, 18 structures. Determined by solution NMR. Released 1 Aug 1996.
Explore 1CMR in 3D Show helices and sheets RCSB PDB PDBe
1CMR 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 | 4-6 | 3 | |
| β-strand | 22-24 | 3 | 1 |
| β-strand | 26-27 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Charybdotoxin, alpha chimera | A | protein | 31 | P13487 (AlphaFold model) |
>1CMR_1 CHARYBDOTOXIN, ALPHA CHIMERA (chains A) CTTSKECWSVCQRLHNTSKGWCDHRGCICES
Transfer of a beta-hairpin from the functional site of snake curaremimetic toxins to the alpha/beta scaffold of scorpion toxins: three-dimensional solution structure of the chimeric protein. Zinn-Justin, S., Guenneugues, M., Drakopoulou, E. et al. Biochemistry (1996) 35:8535-8543. DOI 10.1021/bi960466n · 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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