NMR structure of omega-conotoxin mviia: no constraints on disulphide bridges. Determined by solution NMR. Released 1 Mar 2000.
Explore 1DW5 in 3D Show helices and sheets RCSB PDB PDBe
1DW5 contains 0 α-helices 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 | 1 | 1 |
| β-strand | 15 | 1 | 1 |
| β-strand | 21 | 1 | 2 |
| β-strand | 24 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Omega-conotoxin mviia | A | protein | 26 | P05484 (AlphaFold model) |
>1DW5_1 OMEGA-CONOTOXIN MVIIA (chains A) CKGKGAKCSRLMYDCCTGSCRSGKCX
Structural and dynamic characterization of omega-conotoxin MVIIA: the binding loop exhibits slow conformational exchange. Atkinson, R.A., Kieffer, B., Dejaegere, A. et al. Biochemistry (2000) 39:3908-3919. DOI 10.1021/bi992651h · PubMed
Other PDB entries of the same protein (UniProt P05484 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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