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Vaccinia virus E2

Analyse Vaccinia virus E2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7PHY
Type
protein
Length
732 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein E2
UniProt
P21604
Pockets
6 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein E2protein73259% helix, 5% strandP21604

Ligands and binding sites

  • GOL · Glycerol · additive · 5 copies · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1520.650.9515empty
25560.630.7556empty
33480.580.7637GOL
4550.410.8218empty
5740.410.7913empty

Modifications

Observed in the structure: 1 disulfide, 1 modified (disulfide, nonstandard).

Compared structures

  • 7PHY · Vaccinia virus E2 · the same entry in another collection · chain A against A, TM-score 1.00

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