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Chikungunya E1 E2 envelope glycoproteins fitted in semliki forest virus cryo-EM MAP

Analyse Chikungunya E1 E2 envelope glycoproteins fitted in semliki forest virus cryo-EM… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2XFC
Type
protein
Length
2,896 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E1 envelope glycoprotein; E2 envelope glycoprotein
UniProt
Q1H8W5
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 2 distinct chains · 3% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, F, HE1 envelope glycoproteinprotein3904% helix, 44% strandQ1H8W5
B, E, G, IE2 envelope glycoproteinprotein3342% helix, 50% strandQ1H8W5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19250.850.86100empty
210830.840.8574empty
310450.840.8579empty
48230.730.7858empty
58540.720.7759empty

Interfaces

12 interfaces between chains.

  • F–G · 2743 Ų buried · 43 hydrogen bonds · protein-protein
  • A–B · 2611 Ų buried · 54 hydrogen bonds · protein-protein
  • H–I · 2542 Ų buried · 46 hydrogen bonds · protein-protein
  • D–E · 2541 Ų buried · 37 hydrogen bonds · protein-protein
  • D–I · 663 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 56 disulfide (disulfide).

Compared structures

  • 2XFC · CHIKUNGUNYA E1 E2 ENVELOPE GLYCOPROTEINS FITTED IN SEMLIKI FOREST VIRUS cryo-EM MAP · the same entry in another collection · chain A against A, TM-score 1.00

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