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Structure of the epstein-barr virus GP42 protein bound to the MHC class II receptor HLA-DR1

Analyse Structure of the epstein-barr virus GP42 protein bound to the MHC class II… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1KG0
Type
protein
Length
517 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MHC class II receptor HLA-DR1; Hemagglutinin ha peptide; GP42 protein
UniProt
P01903, P04229, P03205
Pockets
4 · best druggability 0.41

Structure

x-ray diffraction · 4 distinct chains · 14% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMHC class II receptor HLA-DR1protein18014% helix, 46% strandP01903
BMHC class II receptor HLA-DR1protein18818% helix, 46% strandP04229
DHemagglutinin ha peptideprotein130% helix, 8% strand—
CGP42 proteinprotein13611% helix, 24% strandP03205

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11500.410.7318empty
2850.330.7417empty
3650.310.7514empty
4740.300.7321empty

Interfaces

4 interfaces between chains.

  • A–B · 2565 Ų buried · 38 hydrogen bonds · protein-protein
  • A–D · 688 Ų buried · 12 hydrogen bonds · protein-protein
  • B–D · 682 Ų buried · 9 hydrogen bonds · protein-protein
  • B–C · 547 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 1KG0 · Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor… · the same entry in another collection · chain A against A, TM-score 1.00
  • P01903 · AlphaFold monomer V2.0 prediction for HLA class II histocompatibility antigen, dr alpha… · a predicted model of the same protein · chain A against A, TM-score 0.97

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