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Structure of japanese encephalitis virus

Analyse Structure of japanese encephalitis virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5WSN
Type
protein
Length
1,722 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E protein; M protein
UniProt
A1E4C6, Q82863
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 2 distinct chains · 26% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, EE proteinprotein50021% helix, 34% strandA1E4C6
B, D, FM proteinprotein7459% helix, 0% strandQ82863

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110970.860.87127empty
23170.730.8545empty
310180.720.7581empty
44880.710.8054empty
53730.680.8146empty

Interfaces

9 interfaces between chains.

  • E–F · 1431 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 1423 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 1389 Ų buried · 11 hydrogen bonds · protein-protein
  • C–E · 1196 Ų buried · 2 hydrogen bonds · protein-protein
  • D–F · 802 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 15 disulfide (disulfide).

Compared structures

  • 5WSN · Structure of Japanese encephalitis virus · the same entry in another collection · chain A against A, TM-score 1.00

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