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Association of the pr peptides with dengue virus blocks membrane fusion at acidic pH

Analyse Association of the pr peptides with dengue virus blocks membrane fusion at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3IYA
Type
protein
Length
1,421 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Envelope protein; Prm protein
UniProt
P18356
Pockets
2 · best druggability 0.31

Structure

electron microscopy · 3 distinct chains · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEnvelope proteinprotein3920% helix, 0% strandP18356
D, E, FPrm proteinprotein810% helix, 0% strandP18356
B, CEnvelope proteinprotein3930% helix, 0% strandP18356

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1710.310.7218empty
2550.290.7323empty

Interfaces

6 interfaces between chains.

  • B–C · 911 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 330 Ų buried · 0 hydrogen bonds · protein-protein
  • C–F · 159 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 158 Ų buried · 0 hydrogen bonds · protein-protein
  • B–E · 158 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3IYA · Association of the pr peptides with dengue virus blocks membrane fusion at acidic pH · the same entry in another collection · chain A against A, TM-score 1.00

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