Solution structure of stereo-array isotope labelled (SAIL) C-terminal dimerization domain of SARS coronavirus nucleocapsid protein. Determined by solution NMR. Released 26 Aug 2008.
Explore 2JW8 in 3D Show helices and sheets RCSB PDB PDBe
2JW8 contains 19 α-helices and 4 β-strands across 2 chains. 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 | 252-255 | 4 | |
| α-helix | 271-274 | 4 | |
| α-helix | 292-295 | 4 | |
| α-helix | 296-298 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 309-311 | 3 | |
| α-helix | 312-315 | 4 | |
| β-strand | 322-326 | 5 | 1 |
| β-strand | 329-339 | 11 | 1 |
| α-helix | 347-358 | 12 | |
| α-helix | 360-363 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 253-255 | 3 | |
| α-helix | 271-274 | 4 | |
| α-helix | 282-284 | 3 | |
| α-helix | 292-295 | 4 | |
| α-helix | 296-298 | 3 | |
| α-helix | 303-306 | 4 | |
| α-helix | 309-311 | 3 | |
| α-helix | 312-315 | 4 | |
| β-strand | 322-326 | 5 | 1 |
| β-strand | 329-338 | 10 | 1 |
| α-helix | 347-360 | 14 | |
| α-helix | 361-363 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleocapsid protein | A, B | protein | 128 | Human SARS coronavirus | P59595 (AlphaFold model) |
>2JW8_1 Nucleocapsid protein (chains A, B) MHHHHHHAMGTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGT DYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKH IDAYKTFP
Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method. Takeda, M., Chang, C.K., Ikeya, T. et al. J Mol Biol (2008) 380:608-622. DOI 10.1016/j.jmb.2007.11.093 · PubMed
Other PDB entries of the same protein (UniProt P59595 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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