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SARS-cov-2 omicron S-open-2

Analyse SARS-cov-2 omicron S-open-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7WVO
Type
protein
Length
2,961 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Spike glycoprotein
UniProt
P0DTC2
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 3 distinct chains · 19% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASpike glycoproteinprotein104818% helix, 30% strandP0DTC2
BSpike glycoproteinprotein105719% helix, 30% strandP0DTC2
CSpike glycoproteinprotein85621% helix, 30% strandP0DTC2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111910.860.87139empty
23820.840.9358empty
33960.840.9240empty
46210.790.8567empty
58040.790.8278empty

Interfaces

3 interfaces between chains.

  • A–B · 5258 Ų buried · 36 hydrogen bonds · protein-protein
  • A–C · 4527 Ų buried · 41 hydrogen bonds · protein-protein
  • B–C · 4304 Ų buried · 30 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 35 disulfide (disulfide).

Compared structures

  • 7WVO · SARS-CoV-2 Omicron S-open-2 · the same entry in another collection · chain A against A, TM-score 1.00

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