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Structure of gc glycoprotein from severe fever with thrombocytopenia syndrome virus in the trimeric postfusion conformation

Analyse Structure of gc glycoprotein from severe fever with thrombocytopenia syndrome… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5G47
Type
protein
Length
1,284 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sftsv gc
UniProt
R4V2Q5
Ligands
NAG, CL
Pockets
19 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CSftsv gcprotein4286% helix, 54% strandR4V2Q5

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B, C
  • CL · Chloride ion · ion · chains A, B, C

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

Pockets

19 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18170.840.8689empty
23580.820.9161empty
31410.810.9826empty
45030.800.8768empty
55010.790.8664empty

Interfaces

3 interfaces between chains.

  • B–C · 2609 Ų buried · 32 hydrogen bonds · protein-protein
  • A–C · 2600 Ų buried · 40 hydrogen bonds · protein-protein
  • A–B · 2516 Ų buried · 39 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 39 disulfide, 3 glycan (disulfide, N-glycosylation).

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