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Post-fusion conformation of the envelope protein of tick-borne encephalitis virus with longer stem

Analyse Post-fusion conformation of the envelope protein of tick-borne encephalitis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6S8C
Type
protein
Length
1,016 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Genome POLYPROTEIN,GENOME polyprotein
EC
3.4.21.91, 3.6.1.15, 3.6.4.13, 2.1.1.56, 2.1.1.57, 2.7.7.48
UniProt
P14336
Pockets
15 · best druggability 0.88

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGenome POLYPROTEIN,GENOME polyprotein (EC 3.4.21.91, 3.6.1.15, 3.6.4.13, 2.1.1.56, 2.1.1.57, 2.7.7.48)protein3318% helix, 47% strandP14336
BGenome POLYPROTEIN,GENOME polyprotein (EC 3.4.21.91, 3.6.1.15, 3.6.4.13, 2.1.1.56, 2.1.1.57, 2.7.7.48)protein3488% helix, 51% strandP14336
CGenome POLYPROTEIN,GENOME polyprotein (EC 3.4.21.91, 3.6.1.15, 3.6.4.13, 2.1.1.56, 2.1.1.57, 2.7.7.48)protein3377% helix, 51% strandP14336

Pockets

15 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16560.880.9349empty
21210.800.9822empty
33210.780.8948empty
410380.780.80117empty
53330.760.8846empty

Interfaces

3 interfaces between chains.

  • A–B · 2095 Ų buried · 36 hydrogen bonds · protein-protein
  • A–C · 2055 Ų buried · 30 hydrogen bonds · protein-protein
  • B–C · 1969 Ų buried · 29 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

  • 6S8C · Post-fusion conformation of the envelope protein of tick-borne encephalitis virus with… · the same entry in another collection · chain A against A, TM-score 1.00

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