2CJR: Nucleocapsid protein
Crystal structure of oligomerization domain of SARS coronavirus nucleocapsid protein. Determined by X-ray diffraction at 2.5 Å resolution. Released 10 Apr 2007.
- Method
- X-ray diffraction
- Resolution
- 2.5 Å
- Organism
- SARS CORONAVIRUS
- Chains
- 8
- Atoms
- 7,973
- Mol. weight
- 116.48 kDa
- Released
- 10 Apr 2007
Explore 2CJR in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2CJR contains 71 α-helices and 40 β-strands across 8 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.
Chain A: 9 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 260-262 | 3 | |
| β-strand | 266 | 1 | 1 |
| β-strand | 269 | 1 | 1 |
| α-helix | 271-275 | 5 | |
| β-strand | 287 | 1 | 2 |
| α-helix | 290-295 | 6 | |
| α-helix | 296-298 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-317 | 6 | |
| β-strand | 322-325 | 4 | 3 |
| β-strand | 330-339 | 10 | 3 |
| α-helix | 347-357 | 11 | |
| β-strand | 358 | 1 | 2 |
| α-helix | 360-362 | 3 | |
Chain B: 8 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 260-262 | 3 | |
| β-strand | 266 | 1 | 4 |
| β-strand | 269 | 1 | 4 |
| α-helix | 271-275 | 5 | |
| α-helix | 290-295 | 6 | |
| α-helix | 296-298 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 312-318 | 7 | |
| β-strand | 320-326 | 7 | 3 |
| β-strand | 329-339 | 11 | 3 |
| α-helix | 347-357 | 11 | |
| α-helix | 360-363 | 4 | |
Chain C: 8 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 260-262 | 3 | |
| β-strand | 266 | 1 | 5 |
| β-strand | 269 | 1 | 5 |
| α-helix | 271-275 | 5 | |
| β-strand | 287 | 1 | 6 |
| α-helix | 290-295 | 6 | |
| α-helix | 296-298 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 312-318 | 7 | |
| β-strand | 320-325 | 6 | 7 |
| β-strand | 330-340 | 11 | 7 |
| α-helix | 347-357 | 11 | |
| β-strand | 358 | 1 | 6 |
| α-helix | 360-363 | 4 | |
Chain D: 10 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 260-262 | 3 | |
| α-helix | 271-275 | 5 | |
| 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 | 7 |
| β-strand | 329-339 | 11 | 7 |
| α-helix | 340 | 1 | |
| α-helix | 347-357 | 11 | |
| α-helix | 360-363 | 4 | |
Chain E: 9 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 260-262 | 3 | |
| α-helix | 271-275 | 5 | |
| β-strand | 278 | 1 | 8 |
| β-strand | 285 | 1 | 8 |
| α-helix | 290-295 | 6 | |
| α-helix | 296-298 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 310-311 | 2 | |
| α-helix | 313-316 | 4 | |
| β-strand | 320-323 | 4 | 9 |
| β-strand | 326 | 1 | 10 |
| β-strand | 329 | 1 | 10 |
| β-strand | 331-339 | 9 | 9 |
| α-helix | 347-357 | 11 | |
| α-helix | 360-362 | 3 | |
Chain F: 10 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 260-262 | 3 | |
| α-helix | 263-265 | 3 | |
| α-helix | 271-275 | 5 | |
| β-strand | 287 | 1 | 11 |
| α-helix | 290-295 | 6 | |
| α-helix | 296-298 | 3 | |
| α-helix | 302-305 | 4 | |
| α-helix | 306-308 | 3 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-318 | 7 | |
| β-strand | 320-324 | 5 | 9 |
| β-strand | 331-339 | 9 | 9 |
| α-helix | 349-357 | 9 | |
| β-strand | 358 | 1 | 11 |
Chain G: 9 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 260-262 | 3 | |
| α-helix | 271-275 | 5 | |
| β-strand | 278 | 1 | 12 |
| β-strand | 285 | 1 | 12 |
| 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 | 13 |
| β-strand | 330-339 | 10 | 13 |
| α-helix | 345-347 | 3 | |
| α-helix | 349-358 | 10 | |
Chain H: 8 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 260-262 | 3 | |
| β-strand | 266 | 1 | 14 |
| β-strand | 269 | 1 | 14 |
| α-helix | 271-275 | 5 | |
| β-strand | 278 | 1 | 15 |
| β-strand | 285 | 1 | 15 |
| β-strand | 287 | 1 | 16 |
| 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 | 320-324 | 5 | 13 |
| β-strand | 331-339 | 9 | 13 |
| α-helix | 347-357 | 11 | |
| β-strand | 358 | 1 | 16 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Nucleocapsid protein | A, B, C, D, E, F, G, H | protein | 128 | SARS CORONAVIRUS | P59595 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>2CJR_1 NUCLEOCAPSID PROTEIN (chains A, B, C, D, E, F, G, H)
MHHHHHHAMGTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGT
DYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKH
IDAYKTFP
Primary citation
Structure of the Sars Coronavirus Nucleocapsid Protein RNA-Binding Dimerization Domain Suggests a Mechanism for Helical Packaging of Viral RNA. Chen, C.-Y., Chang, C.K., Chang, Y.W. et al. J Mol Biol (2007) 368:1075. DOI 10.1016/J.JMB.2007.02.069 · PubMed
Other PDB entries of the same protein (UniProt P59595 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2OFZ 1.17 Å, Ultrahigh Resolution Crystal Structure of RNA Binding Domain of SARS Nucleopcapsid (N…
- 1X7Q 1.45 Å, Crystal structure of HLA-A*1101 with sars nucleocapsid peptide
- 2GIB 1.75 Å, Crystal structure of the SARS coronavirus nucleocapsid protein dimerization domain
- 2OG3 1.85 Å, structure of the rna binding domain of n protein from SARS coronavirus in cubic crystal…
- 7LG0 2.3 Å, Human leukocyte antigen B*07:02 in complex with SARS-CoV2 epitope SPRWYFYYL
- 6IEX 2.31 Å, Crystal structure of HLA-B*4001 in complex with SARS-CoV derived peptide N216-225…
- 3I6L 2.4 Å, Newly identified epitope N1 derived from SARS-CoV N protein complexed with HLA-A*2402
- 1SSK Structure of the N-terminal RNA-binding Domain of the SARS CoV Nucleocapsid Protein
- 2JW8 Solution structure of stereo-array isotope labelled (SAIL) C-terminal dimerization…
Browse structure collections
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