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MolNFT v1 · #72229 · protein

Molecular basis of the inhibition of henipa viruses

3N27 · Fusion glycoprotein F0, linker, fusion glycoprotein F0: “Molecular basis of the inhibition of henipa viruses”. X-ray diffraction, 1 pocket (best druggability 0.72). MolNFT v1 #72229 on GenesisL1: 3D structure, binding sites and…

PDB
3N27
Type
protein
Length
222 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fusion glycoprotein F0, linker, fusion glycoprotein F0
UniProt
Q9IH63
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · 3 distinct chains · 89% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFusion glycoprotein F0, linker, fusion glycoprotein F0protein7388% helix, 0% strandQ9IH63
BFusion glycoprotein F0, linker, fusion glycoprotein F0protein7987% helix, 0% strandQ9IH63
CFusion glycoprotein F0, linker, fusion glycoprotein F0protein7091% helix, 0% strandQ9IH63

Ligands and binding sites

  • TBU · Tertiary-butyl alcohol · additive · 2 copies · chains A, B, C
  • CIT · Citric acid · additive

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1560.720.9814TBU

Interfaces

3 interfaces between chains.

  • A–B · 1298 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 1293 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 1274 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 3N27 · Molecular Basis of the Inhibition of Henipa Viruses · the same entry in another collection · chain C against C, TM-score 1.00

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