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Cryo-EM structure of sads-cov spike

Analyse Cryo-EM structure of sads-cov spike in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6M39
Type
protein
Length
2,811 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Spike glycoprotein
UniProt
A0A2P1G7F5
Ligands
NAG
Pockets
20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 19% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CSpike glycoproteinprotein93719% helix, 26% strandA0A2P1G7F5

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 54 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
19310.880.90122empty
211380.870.88143empty
33490.860.9559empty
410770.860.87123empty
56540.830.8887empty

Interfaces

3 interfaces between chains.

  • B–C · 6285 Ų buried · 76 hydrogen bonds · protein-protein
  • A–B · 6275 Ų buried · 76 hydrogen bonds · protein-protein
  • A–C · 6267 Ų buried · 76 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 54 glycan, 30 disulfide (N-glycosylation, disulfide).

Compared structures

  • 6M39 · Cryo-EM structure of SADS-CoV spike · the same entry in another collection · chain A against A, TM-score 1.00

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