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Crystal structure of GP2 from lassa virus in a post fusion conformation

Analyse Crystal structure of GP2 from lassa virus in a post fusion conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5OMI
Type
protein
Length
325 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pre-glycoprotein polyprotein gp complex
UniProt
A0A097F3Y1
Ligands
NAG, NA, CL
Pockets
4 · best druggability 0.52

Structure

x-ray diffraction · 3 distinct chains · 71% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APre-glycoprotein polyprotein gp complexprotein10772% helix, 2% strandA0A097F3Y1
BPre-glycoprotein polyprotein gp complexprotein10873% helix, 2% strandA0A097F3Y1
CPre-glycoprotein polyprotein gp complexprotein11069% helix, 2% strandA0A097F3Y1

Ligands and binding sites

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

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
11980.520.7727empty
22030.520.7738empty
3950.440.7919empty
41010.430.7822empty

Interfaces

3 interfaces between chains.

  • B–C · 1805 Ų buried · 15 hydrogen bonds · protein-protein
  • A–C · 1729 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 1700 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 5OMI · Crystal structure of GP2 from Lassa virus in a post fusion conformation · the same entry in another collection · chain A against A, TM-score 1.00

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