SARS-CoV-2 nucleocapsid C-terminal domain in complex with BCY00018176. Determined by X-ray diffraction at 1.46 Å resolution. Released 4 Mar 2026.
Explore 9RXL in 3D Show helices and sheets RCSB PDB PDBe
9RXL contains 24 α-helices and 14 β-strands across 4 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 | 5-9 | 5 | |
| α-helix | 13-14 | 2 | |
| β-strand | 15 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 251-254 | 4 | |
| α-helix | 259-261 | 3 | |
| β-strand | 265 | 1 | 2 |
| β-strand | 268 | 1 | 2 |
| α-helix | 270-274 | 5 | |
| β-strand | 286 | 1 | 3 |
| α-helix | 289-294 | 6 | |
| α-helix | 295-297 | 3 | |
| α-helix | 301-305 | 5 | |
| α-helix | 309-310 | 2 | |
| α-helix | 311-317 | 7 | |
| β-strand | 319-325 | 7 | 1 |
| β-strand | 328-338 | 11 | 1 |
| α-helix | 346-356 | 11 | |
| β-strand | 357 | 1 | 3 |
| α-helix | 359-362 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 252-255 | 4 | |
| α-helix | 259-261 | 3 | |
| β-strand | 265 | 1 | 4 |
| β-strand | 268 | 1 | 4 |
| α-helix | 270-274 | 5 | |
| β-strand | 286 | 1 | 5 |
| α-helix | 289-294 | 6 | |
| α-helix | 295-297 | 3 | |
| α-helix | 301-305 | 5 | |
| α-helix | 309-310 | 2 | |
| α-helix | 311-317 | 7 | |
| β-strand | 319-325 | 7 | 1 |
| β-strand | 328-338 | 11 | 1 |
| α-helix | 346-356 | 11 | |
| β-strand | 357 | 1 | 5 |
| α-helix | 359-362 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| BCY00018176 | A, B | protein | 18 | Homo sapiens | |
| Nucleoprotein | C, D | protein | 139 | Severe acute respiratory syndrome coronavirus 2 | P0DTC9 (AlphaFold model) |
>9RXL_1 BCY00018176 (chains A, B) ACRVNPCILTGINIPCAX
>9RXL_2 Nucleoprotein (chains C, D) GSTKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQI AQFAPSASAFFGMSRIGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFP GSSGLNDIFEAQKIEWHEA
| ID | Name | Formula | Copies |
|---|---|---|---|
| LFI | 1-[3,5-bis(3-bromanylpropanoyl)-1,3,5-triazinan-1-yl]-3-bromanyl-propan-1-one | C12 H18 Br3 N3 O3 | 2 |
Water and common crystallization additives (GOL) are not listed.
Utilizing Constrained Bicyclic Peptides for In Vitro Diagnostics. Shamsabadi, A., Creamer, A., Sadler, C.J. et al. ACS Nano (2026) 20:5928-5939. DOI 10.1021/acsnano.5c19041 · PubMed
Other PDB entries of the same protein (UniProt P0DTC9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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