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Crystal structure of hendra virus fusion core

Analyse Crystal structure of hendra virus fusion core in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WP8
Type
protein
Length
191 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fusion glycoprotein F0,FUSION glycoprotein F0
UniProt
O89342
Pockets
1 · best druggability 0.76

Structure

x-ray diffraction · 3 distinct chains · 91% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFusion glycoprotein F0,FUSION glycoprotein F0protein6489% helix, 0% strandO89342
BFusion glycoprotein F0,FUSION glycoprotein F0protein6491% helix, 0% strandO89342
CFusion glycoprotein F0,FUSION glycoprotein F0protein6392% helix, 0% strandO89342

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1720.760.9918empty

Interfaces

3 interfaces between chains.

  • A–C · 993 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 954 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 907 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 1WP8 · crystal structure of Hendra Virus fusion core · the same entry in another collection · chain A against A, TM-score 1.00

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