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Acidic omicron spike trimer

Analyse Acidic omicron spike trimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7WG7
Type
protein
Length
3,313 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Spike glycoprotein
UniProt
P0DTC2
Ligands
NAG, BMA
Pockets
20 · best druggability 0.89

Structure

electron microscopy · 2 distinct chains · 20% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, ASpike glycoproteinprotein109820% helix, 26% strandP0DTC2
CSpike glycoproteinprotein111720% helix, 23% strandP0DTC2

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 68 copies · chains B, A, C
  • BMA · beta-D-mannopyranose · sugar · 5 copies

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19210.890.91108empty
28480.870.90102empty
38680.810.8484empty
45910.800.8683empty
52550.790.9150empty

Interfaces

3 interfaces between chains.

  • A–C · 5833 Ų buried · 33 hydrogen bonds · protein-protein
  • B–A · 5345 Ų buried · 26 hydrogen bonds · protein-protein
  • B–C · 4554 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 44 glycan, 39 disulfide (N-glycosylation, disulfide, glycosylation).

Compared structures

  • 7WG7 · Acidic Omicron Spike Trimer · the same entry in another collection · chain B against B, TM-score 1.00

Analyse

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