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Potent neutralizing nanobodies resist convergent circulating variants of SARS-cov-2 by targeting novel and conserved epitopes-covs with NB95

Analyse Potent neutralizing nanobodies resist convergent circulating variants of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7N9C
Type
protein
Length
3,019 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Spike glycoprotein; Nanobody NB95
UniProt
P0DTC2
Pockets
20 · best druggability 0.83

Structure

electron microscopy · 4 distinct chains · 23% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASpike glycoproteinprotein98023% helix, 31% strandP0DTC2
BSpike glycoproteinprotein81225% helix, 31% strandP0DTC2
CSpike glycoproteinprotein97524% helix, 31% strandP0DTC2
D, ENanobody NB95protein1260% helix, 33% strand—

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111180.830.84122empty
210560.830.84105empty
34050.820.9058empty
410590.790.8192empty
57360.780.8262empty

Interfaces

5 interfaces between chains.

  • A–C · 4300 Ų buried · 32 hydrogen bonds · protein-protein
  • A–B · 4280 Ų buried · 36 hydrogen bonds · protein-protein
  • B–C · 3969 Ų buried · 33 hydrogen bonds · protein-protein
  • A–E · 849 Ų buried · 11 hydrogen bonds · protein-protein
  • C–D · 647 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 35 disulfide (disulfide).

Compared structures

  • 7N9C · Potent neutralizing nanobodies resist convergent circulating variants of SARS-CoV-2 by… · the same entry in another collection · chain A against A, TM-score 1.00

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