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Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain

Analyse Cryo-EM structure of the prefusion state of canine distemper virus fusion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6XYE
Type
protein
Length
1,293 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
4.3
Source
Canine morbillivirus
Molecule
Fusion glycoprotein F2; Fusion glycoprotein F1
UniProt
Q9YKL7
Pockets
20 · best druggability 0.78

Structure

electron microscopy · resolution 4.3 · 2 distinct chains · 28% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, EFusion glycoprotein F2protein7443% helix, 23% strandQ9YKL7
B, D, FFusion glycoprotein F1protein35725% helix, 23% strandQ9YKL7

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17520.780.82113empty
211560.780.79113empty
34650.730.8256empty
45550.690.7871empty
53900.690.8138empty

Interfaces

12 interfaces between chains.

  • E–F · 4177 Ų buried · 44 hydrogen bonds · protein-protein
  • A–B · 4174 Ų buried · 44 hydrogen bonds · protein-protein
  • C–D · 4163 Ų buried · 44 hydrogen bonds · protein-protein
  • B–F · 2203 Ų buried · 21 hydrogen bonds · protein-protein
  • B–D · 2177 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 disulfide (disulfide).

Compared structures

  • 6XYE · Cryo-EM structure of the prefusion state of canine distemper virus fusion protein… · the same entry in another collection · chain A against A, TM-score 1.00

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