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Mink Variant SARS-CoV-2 Spike in Closed conformation

Analyse Mink Variant SARS-CoV-2 Spike in Closed conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7R18
Type
protein
Length
3,189 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.0
Source
Severe acute respiratory syndrome coronavirus 2
Molecule
Spike glycoprotein
UniProt
P0DTC2
Ligands
NAG, FUC
Pockets
20 · best druggability 0.88

Structure

electron microscopy · resolution 3.0 · 1 distinct chain · 20% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CSpike glycoproteinprotein106320% helix, 33% strandP0DTC2

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 57 copies · chains A, B, C
  • FUC · alpha-L-fucopyranose · sugar · 3 copies · chains A, B, C

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
111510.880.89117empty
211920.850.86144empty
39780.810.8276empty
410620.810.8280empty
59100.810.8370empty

Interfaces

3 interfaces between chains.

  • B–C · 4348 Ų buried · 34 hydrogen bonds · protein-protein
  • A–B · 4348 Ų buried · 34 hydrogen bonds · protein-protein
  • A–C · 4337 Ų buried · 34 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 48 glycan, 42 disulfide (N-glycosylation, disulfide).

Compared structures

  • 7R18 · Mink variant SARS-cov-2 spike in closed conformation · the same entry in another collection · chain A against A, TM-score 1.00

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