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Cryoem structure of chimeric eastern equine encephalitis virus with Fab of eeev-58 antibody

Analyse Cryoem structure of chimeric eastern equine encephalitis virus with Fab of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6MWV
Type
protein
Length
4,616 residues
Chains
16
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E1; E2; Eeev-58 antibody heavy chain; Eeev-58 antibody light chain
UniProt
E9KXM2, E9KXL2, G0YP42
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 4 distinct chains · 4% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, E, I, ME1protein4003% helix, 29% strandE9KXM2
B, F, J, NE2protein3251% helix, 37% strandE9KXL2
C, G, K, OEeev-58 antibody heavy chainprotein2188% helix, 55% strand—
D, H, L, PEeev-58 antibody light chainprotein2116% helix, 55% strandG0YP42

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17920.840.8787empty
29030.840.85100empty
36660.830.8865empty
45710.800.8692empty
59480.780.8087empty

Interfaces

24 interfaces between chains.

  • A–B · 2637 Ų buried · 35 hydrogen bonds · protein-protein
  • E–F · 2630 Ų buried · 35 hydrogen bonds · protein-protein
  • I–J · 2620 Ų buried · 34 hydrogen bonds · protein-protein
  • M–N · 2617 Ų buried · 36 hydrogen bonds · protein-protein
  • O–P · 1865 Ų buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 72 disulfide, 2 isopeptide (disulfide, isopeptide).

Compared structures

  • 6MWV · CryoEM structure of Chimeric Eastern Equine Encephalitis Virus with Fab of EEEV-58… · the same entry in another collection · chain A against A, TM-score 1.00

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