Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications. Determined by solution NMR. Released 15 Jul 1993.
Explore 2CRD in 3D Show helices and sheets RCSB PDB PDBe
2CRD contains 1 α-helix and 3 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 | 1 | 1 |
| α-helix | 11-20 | 10 | |
| β-strand | 26-28 | 3 | 1 |
| β-strand | 33-35 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Charybdotoxin | A | protein | 37 | Leiurus quinquestriatus hebraeus | P13487 (AlphaFold model) |
>2CRD_1 CHARYBDOTOXIN (chains A) QFTNVSCTTSKECWSVCQRLHNTSRGKCMNKKCRCYS
Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications. Bontems, F., Gilquin, B., Roumestand, C. et al. Biochemistry (1992) 31:7756-7764. DOI 10.1021/bi00149a003 · 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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