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Structure of the SARS-cov-2 N protein RNA-binding domain bound to single-domain antibody C2

Analyse Structure of the SARS-cov-2 N protein RNA-binding domain bound to single-domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7N0R
Type
protein
Length
500 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nucleoprotein; Single-domain antibody C2
UniProt
P0DTC9
Ligands
SO4
Pockets
7 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BNucleoproteinprotein1272% helix, 24% strandP0DTC9
C, DSingle-domain antibody C2protein12310% helix, 44% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14350.720.8239SO4
21460.500.7928empty
31030.430.7818empty
41240.400.7517empty
5890.340.7417empty

Interfaces

5 interfaces between chains.

  • B–D · 823 Ų buried · 14 hydrogen bonds · protein-protein
  • A–C · 821 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 670 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 162 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 143 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 7N0R · Structure of the SARS-CoV-2 N protein RNA-binding domain bound to single-domain antibody… · the same entry in another collection · chain A against A, TM-score 1.00

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