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Crystal structure of stabilized gp from makona variant of ebola virus

Analyse Crystal structure of stabilized gp from makona variant of ebola virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6VKM
Type
protein
Length
353 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Virion spike glycoprotein
UniProt
A0A2I4PEY8, A0A0E3XL33
Ligands
NAG
Pockets
4 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVirion spike glycoproteinprotein35321% helix, 29% strandA0A2I4PEY8, A0A0E3XL33

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1560.660.9518empty
21390.600.8424empty
3930.380.7620empty
4770.360.7617empty

Modifications

Observed in the structure: 5 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 6VKM · Crystal Structure of Stabilized GP from Makona Variant of Ebola Virus · the same entry in another collection · chain A against A, TM-score 1.00

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