NMR Structure of the N-terminal Coiled Coil Domain of the Andes Hantavirus Nucleocapsid Protein. Determined by solution NMR. Released 5 Aug 2008.
Explore 2K48 in 3D Show helices and sheets RCSB PDB PDBe
2K48 contains 3 α-helices 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 | 10-12 | 3 | |
| α-helix | 32-67 | 36 | |
| α-helix | 71-105 | 35 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoprotein | A | protein | 107 | Andes virus | P11207 (AlphaFold model) |
>2K48_1 Nucleoprotein (chains A) MHHHHHHGKPIPNPLLGLDSTENLYFQGIDPFTMSTLQELQENITAHEQQLVTARQKLKD AEKAVEVDPDDVNKSTLQNRRAAVSTLETKLGELKRQLADLVAAQKL
NMR Structure of the N-terminal Coiled Coil Domain of the Andes Hantavirus Nucleocapsid Protein. Wang, Y., Boudreaux, D.M., Estrada, D.F. et al. J Biol Chem (2008) 283:28297-28304. DOI 10.1074/jbc.M804869200 · PubMed
Other PDB entries of the same protein (UniProt P11207 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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