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Cryo-EM structure of the SARS-cov-2 HR1HR2 fusion core complex with A942S mutation

Analyse Cryo-EM structure of the SARS-cov-2 HR1HR2 fusion core complex with A942S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7RZU
Type
protein
Length
324 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SARS-cov-2 HR1 A942S linked to a SCAFFOLD,SPIKE protein S2'; Spike protein S2'
UniProt
P0DTC2
Pockets
1 · best druggability 0.64

Structure

electron microscopy · 2 distinct chains · 80% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CSARS-cov-2 HR1 A942S linked to a SCAFFOLD,SPIKE protein S2'protein7197% helix, 0% strandP0DTC2
D, E, FSpike protein S2'protein3746% helix, 0% strandP0DTC2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1610.640.9312empty

Interfaces

9 interfaces between chains.

  • C–F · 1193 Ų buried · 12 hydrogen bonds · protein-protein
  • B–E · 1192 Ų buried · 12 hydrogen bonds · protein-protein
  • A–D · 1185 Ų buried · 12 hydrogen bonds · protein-protein
  • C–E · 1165 Ų buried · 15 hydrogen bonds · protein-protein
  • B–D · 1164 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 7RZU · Cryo-EM structure of the SARS-CoV-2 HR1HR2 fusion core complex with A942S mutation · the same entry in another collection · chain A against A, TM-score 1.00

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