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Rsv prefusion F bound to RSD5 Fab

Analyse Rsv prefusion F bound to RSD5 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6DC3
Type
protein
Length
894 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab RSD5-germline heavy chain; Fab RSD5-germline light chain; Rsv fusion glycoprotein
UniProt
Q6N089, Q8N355, P03420, M1E1E4
Ligands
NAG, SO4
Pockets
7 · best druggability 0.61

Structure

x-ray diffraction · 3 distinct chains · 19% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HFab RSD5-germline heavy chainprotein2299% helix, 48% strandQ6N089
LFab RSD5-germline light chainprotein2135% helix, 51% strandQ8N355
FRsv fusion glycoproteinprotein45231% helix, 33% strandP03420, M1E1E4

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains F
  • SO4 · Sulfate ion · ion · 13 copies · chains H, L, F

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13330.610.7851empty
24590.580.7450empty
32070.530.7721empty
41170.460.7920empty
5960.440.7915empty

Interfaces

3 interfaces between chains.

  • H–L · 1971 Ų buried · 20 hydrogen bonds · protein-protein
  • H–F · 643 Ų buried · 8 hydrogen bonds · protein-protein
  • L–F · 311 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 6DC3 · RSV prefusion F bound to RSD5 Fab · the same entry in another collection · chain H against H, TM-score 1.00

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