9RXL: SARS-CoV-2 nucleocapsid C-terminal domain

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.

Method
X-ray diffraction
Resolution
1.46 Å
Organisms
Homo sapiens, Severe acute respiratory syndrome coronavirus 2
Chains
4
Atoms
2,511
Mol. weight
35.72 kDa
Ligands
LFI
Released
4 Mar 2026

Explore 9RXL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A and B: 2 helices, 1 β-strand

ElementResiduesLengthSheet
α-helix5-95
α-helix13-142
β-strand1511
Chain C: 10 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix251-2544
α-helix259-2613
β-strand26512
β-strand26812
α-helix270-2745
β-strand28613
α-helix289-2946
α-helix295-2973
α-helix301-3055
α-helix309-3102
α-helix311-3177
β-strand319-32571
β-strand328-338111
α-helix346-35611
β-strand35713
α-helix359-3624
Chain D: 10 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix252-2554
α-helix259-2613
β-strand26514
β-strand26814
α-helix270-2745
β-strand28615
α-helix289-2946
α-helix295-2973
α-helix301-3055
α-helix309-3102
α-helix311-3177
β-strand319-32571
β-strand328-338111
α-helix346-35611
β-strand35715
α-helix359-3624

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
BCY00018176A, Bprotein18Homo sapiens
NucleoproteinC, Dprotein139Severe acute respiratory syndrome coronavirus 2P0DTC9 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9RXL_1 BCY00018176 (chains A, B)
ACRVNPCILTGINIPCAX
Sequence of entity 2 (C, D), FASTA
>9RXL_2 Nucleoprotein (chains C, D)
GSTKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQI
AQFAPSASAFFGMSRIGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFP
GSSGLNDIFEAQKIEWHEA

Ligands and cofactors

IDNameFormulaCopies
LFI1-[3,5-bis(3-bromanylpropanoyl)-1,3,5-triazinan-1-yl]-3-bromanyl-propan-1-oneC12 H18 Br3 N3 O32

Water and common crystallization additives (GOL) are not listed.

Primary citation

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:

Browse structure collections

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