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Rift valley fever virus gn in complex with a neutralizing antibody fragment

Analyse Rift valley fever virus gn in complex with a neutralizing antibody fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6I9I
Type
protein
Length
955 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rv-GN1 heavy chain; Rv-GN1 light chain; Glycoprotein
UniProt
A2T080
Pockets
10 · best druggability 0.78

Structure

x-ray diffraction · 6 distinct chains · 6% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARv-GN1 heavy chainprotein2084% helix, 50% strand—
BRv-GN1 light chainprotein2166% helix, 52% strand—
CGlycoproteinprotein5217% helix, 29% strandA2T080
DGlycoproteinprotein5118% helix, 29% strandA2T080
HRv-GN1 heavy chainprotein2134% helix, 49% strand—
LRv-GN1 light chainprotein2156% helix, 53% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19190.780.8077empty
23210.600.7741empty
31450.510.8030empty
4760.460.8227empty
5950.370.7529empty

Interfaces

10 interfaces between chains.

  • A–B · 1873 Ų buried · 20 hydrogen bonds · protein-protein
  • H–L · 1866 Ų buried · 20 hydrogen bonds · protein-protein
  • D–H · 641 Ų buried · 11 hydrogen bonds · protein-protein
  • A–C · 637 Ų buried · 12 hydrogen bonds · protein-protein
  • D–L · 302 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

  • 6I9I · Rift valley fever virus Gn in complex with a neutralizing antibody fragment · the same entry in another collection · chain A against A, TM-score 1.00

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