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Structure of rvfv envelope protein gc in postfusion conformation in complex with mes

Analyse Structure of rvfv envelope protein gc in postfusion conformation in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6EGT
Type
protein
Length
1,334 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycoprotein
UniProt
A2T087
Ligands
NAG, FUL
Pockets
17 · best druggability 0.90

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 57% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGlycoproteinprotein4454% helix, 57% strandA2T087
CGlycoproteinprotein4444% helix, 56% strandA2T087

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A, C, B
  • FUL · beta-L-fucopyranose · sugar · chains A
  • MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains B, C

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

Pockets

17 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18160.900.93110empty
21740.810.9643empty
33260.760.8757empty
43590.740.8660empty
53170.740.8644empty

Interfaces

3 interfaces between chains.

  • A–C · 2935 Ų buried · 49 hydrogen bonds · protein-protein
  • A–B · 2912 Ų buried · 48 hydrogen bonds · protein-protein
  • B–C · 2865 Ų buried · 53 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 36 disulfide, 9 glycan (disulfide, N-glycosylation).

Compared structures

  • 6EGT · Structure of RVFV envelope protein Gc in postfusion conformation in complex with MES · the same entry in another collection · chain A against A, TM-score 1.00

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