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Structure of the hepatitis C virus envelope glycoprotein E2 antigenic 2 region 412-423 bound to the broadly neutralizing antibody HC33.1

Analyse Structure of the hepatitis C virus envelope glycoprotein E2 antigenic 2 region… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4XVJ
Type
protein
Length
264 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
HCV E2 antigen; Antibody heavy chain variable domain; Antibody light chain variable domain
Pockets
1 · best druggability 0.45

Structure

x-ray diffraction · 3 distinct chains · 4% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHCV E2 antigenprotein130% helix, 15% strand—
HAntibody heavy chain variable domainprotein1372% helix, 50% strand—
LAntibody light chain variable domainprotein1147% helix, 46% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11660.450.7530empty

Interfaces

3 interfaces between chains.

  • H–L · 927 Ų buried · 10 hydrogen bonds · protein-protein
  • A–H · 821 Ų buried · 15 hydrogen bonds · protein-protein
  • A–L · 209 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 4XVJ · Structure of the hepatitis C virus envelope glycoprotein E2 antigenic 2 region 412-423… · the same entry in another collection · chain A against A, TM-score 1.00

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