The vaccinia virus H3 envelope protein, a major target of neutralizing antibodies, exhibits a glycosyltransferase fold and binds udp-glucose

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).

Ligands and binding sites

• DHL · 2-amino-ethanethiol · ligand · chains A
• MG · Magnesium ion · metal · chains A
• MOH · Methanol · additive · 6 copies · chains A
• EDO · 1,2-ethanediol · additive · 5 copies · chains A
• PG0 · 2-(2-methoxyethoxy)ethanol · additive · 4 copies · chains A
• EOH · Ethanol · additive · 3 copies · chains A
• GOL · Glycerol · additive · 2 copies · chains A
• PDO · 1,3-propandiol · additive · 2 copies · chains A
• POL · N-propanol · additive · chains A

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

Pockets

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

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

• 5EJ0 · The vaccinia virus H3 envelope protein, a major target of neutralizing antibodies… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P07240
• Elsewhere: RCSB PDB 5EJ0 · PDBe 5EJ0 · UniProt P07240