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Cryo-EM structure of dengue virus serotype 2 strain PVP94-07 complexed with human antibody 2D22 Fab at 37 degrees C

Analyse Cryo-EM structure of dengue virus serotype 2 strain PVP94-07 complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5A1Z
Type
protein
Length
2,394 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Envelope protein; Membrane glycoprotein; Antigen-binding fragment of human antibody 2D22…
UniProt
G9FRP5, V5TI05
Pockets
5 · best druggability 0.43

Structure

electron microscopy · 4 distinct chains · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, EEnvelope proteinprotein4950% helix, 0% strandG9FRP5
B, D, FMembrane glycoproteinprotein720% helix, 0% strandV5TI05
G, I, KAntigen-binding fragment of human antibody 2D22 - heavy chainprotein1200% helix, 0% strand—
H, J, LAntigen-binding fragment of human antibody 2D22 - light chainprotein1110% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11450.430.7335empty
2880.350.7328empty
3660.320.7320empty
4760.320.7222empty
5510.270.7220empty

Interfaces

19 interfaces between chains.

  • E–F · 267 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 255 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 248 Ų buried · 0 hydrogen bonds · protein-protein
  • C–E · 235 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 194 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5A1Z · Cryo-EM structure of Dengue virus serotype 2 strain PVP94-07 complexed with human… · the same entry in another collection · chain J against J, TM-score 1.00

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