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Structure of the hepatitis C virus envelope glycoprotein E2 antigenic region 412-423 bound to the broadly neutralizing antibody AP33

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

PDB
4G6A
Type
protein
Length
901 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E2 peptide; AP33 heavy chain; AP33 light chain
UniProt
Q9YK84
Pockets
10 · best druggability 0.69

Structure

x-ray diffraction · 4 distinct chains · 6% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, AE2 peptideprotein120% helix, 50% strandQ9YK84
CAP33 heavy chainprotein2205% helix, 52% strand—
D, LAP33 light chainprotein2186% helix, 52% strand—
HAP33 heavy chainprotein2215% helix, 52% strand—

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18140.690.7674empty
27390.670.7557empty
32400.620.8241empty
4500.510.8823empty
51420.470.7729empty

Interfaces

9 interfaces between chains.

  • H–L · 2140 Ų buried · 19 hydrogen bonds · protein-protein
  • C–D · 2132 Ų buried · 17 hydrogen bonds · protein-protein
  • B–C · 341 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 336 Ų buried · 5 hydrogen bonds · protein-protein
  • A–H · 331 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 4G6A · Structure of the Hepatitis C virus envelope glycoprotein E2 antigenic region 412-423… · the same entry in another collection · chain B against B, TM-score 1.00

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