Crystal structure of the SARS coronavirus nucleocapsid protein dimerization domain. Determined by X-ray diffraction at 1.75 Å resolution. Released 25 Apr 2006.
Explore 2GIB in 3D Show helices and sheets RCSB PDB PDBe
2GIB contains 15 α-helices and 8 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 | 271-275 | 5 | |
| β-strand | 287 | 1 | 1 |
| α-helix | 290-295 | 6 | |
| α-helix | 296-298 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-318 | 7 | |
| β-strand | 320-325 | 6 | 2 |
| β-strand | 330-340 | 11 | 2 |
| α-helix | 347-357 | 11 | |
| β-strand | 358 | 1 | 1 |
| α-helix | 360-363 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 287 | 1 | 3 |
| α-helix | 290-295 | 6 | |
| α-helix | 296-298 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-318 | 7 | |
| β-strand | 320-326 | 7 | 2 |
| β-strand | 329-339 | 11 | 2 |
| α-helix | 347-357 | 11 | |
| β-strand | 358 | 1 | 3 |
| α-helix | 360-363 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleocapsid protein | A, B | protein | 103 | SARS coronavirus | P59595 (AlphaFold model) |
>2GIB_1 Nucleocapsid protein (chains A, B) SANVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTP SGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPK
Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae. Yu, I.M., Oldham, M.L., Zhang, J. et al. J Biol Chem (2006) 281:17134-17139. DOI 10.1074/jbc.M602107200 · 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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