Solution NMR structure of Dynorphin 1-13 bound to Kappa Opioid Receptor. Determined by solution NMR. Released 9 Sept 2015.
Explore 2N2F in 3D Show helices and sheets RCSB PDB PDBe
2N2F contains 1 α-helix and 0 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 | 5-7 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dynorphin A(1-13) | A | protein | 13 | Homo sapiens | P01213 (AlphaFold model) |
>2N2F_1 Dynorphin A(1-13) (chains A) YGGFLRRIRPKLK
NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor. O'Connor, C., White, K.L., Doncescu, N. et al. Proc Natl Acad Sci U S A (2015) 112:11852-11857. DOI 10.1073/pnas.1510117112 · PubMed
Other PDB entries of the same protein (UniProt P01213 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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