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Crystal structure of glycoprotein D of equine herpesvirus type 1

Analyse Crystal structure of glycoprotein D of equine herpesvirus type 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SQJ
Type
protein
Length
472 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycoprotein D
UniProt
G9HV37
Ligands
NAG, MG
Pockets
9 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycoprotein Dprotein23617% helix, 30% strandG9HV37
BGlycoprotein Dprotein23617% helix, 30% strandG9HV37

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12430.680.8535empty
23490.660.8053empty
31220.550.8337empty
41240.530.8231empty
5940.380.7615empty

Interfaces

1 interface between chains.

  • A–B · 1273 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

  • 6SQJ · Crystal structure of glycoprotein D of Equine Herpesvirus Type 1 · the same entry in another collection · chain A against A, TM-score 1.00

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