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Cryo-EM structure of veev vlp at the 5-fold axes

Analyse Cryo-EM structure of veev vlp at the 5-fold axes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7FFO
Type
protein
Length
1,067 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid protein; Assembly protein E3; Spike glycoprotein E2; Spike glycoprotein E1
EC
3.4.21.90
UniProt
P05674
Pockets
13 · best druggability 0.74

Structure

electron microscopy · 4 distinct chains · 14% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
KCapsid protein (EC 3.4.21.90)protein16310% helix, 42% strandP05674
LAssembly protein E3protein5038% helix, 12% strandP05674
NSpike glycoprotein E2protein41216% helix, 39% strandP05674
OSpike glycoprotein E1protein44212% helix, 40% strandP05674

Pockets

13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18850.740.7870empty
23740.680.8139empty
35180.660.7739empty
44450.620.7649empty
5730.540.8620empty

Interfaces

4 interfaces between chains.

  • N–O · 3581 Ų buried · 32 hydrogen bonds · protein-protein
  • L–N · 804 Ų buried · 9 hydrogen bonds · protein-protein
  • K–N · 538 Ų buried · 10 hydrogen bonds · protein-protein
  • K–O · 300 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 13 disulfide (disulfide).

Compared structures

  • 7FFO · Cryo-EM structure of VEEV VLP at the 5-fold axes · the same entry in another collection · chain K against K, TM-score 1.00

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