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Cryoem structure of eastern equine encephalitis (eeev) vlp

Analyse Cryoem structure of eastern equine encephalitis (eeev) vlp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6XO4
Type
protein
Length
3,992 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Togavirin
EC
3.4.21.90
UniProt
Q88678
Pockets
20 · best druggability 0.83

Structure

electron microscopy · 3 distinct chains · 12% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, G, JTogavirin (EC 3.4.21.90)protein43313% helix, 34% strandQ88678
B, E, H, KTogavirin (EC 3.4.21.90)protein41414% helix, 36% strandQ88678
C, F, I, LTogavirin (EC 3.4.21.90)protein1512% helix, 28% strandQ88678

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111120.830.84121empty
210580.830.84114empty
311220.830.84101empty
42350.740.8938empty
55170.730.8277empty

Interfaces

23 interfaces between chains.

  • G–H · 2950 Ų buried · 19 hydrogen bonds · protein-protein
  • D–E · 2929 Ų buried · 21 hydrogen bonds · protein-protein
  • A–B · 2927 Ų buried · 21 hydrogen bonds · protein-protein
  • J–K · 2915 Ų buried · 17 hydrogen bonds · protein-protein
  • E–J · 632 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 36 disulfide (disulfide).

Compared structures

  • 6XO4 · CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP · the same entry in another collection · chain A against A, TM-score 1.00

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