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Crystal structure of the oligomerization domain of VP35 from reston virus

Analyse Crystal structure of the oligomerization domain of VP35 from reston virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GBQ
Type
protein
Length
530 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polymerase cofactor VP35
UniProt
Q8JPY0
Pockets
1 · best druggability 0.64

Structure

x-ray diffraction · 8 distinct chains · 92% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolymerase cofactor VP35protein7096% helix, 0% strandQ8JPY0
BPolymerase cofactor VP35protein6586% helix, 0% strandQ8JPY0
CPolymerase cofactor VP35protein6996% helix, 0% strandQ8JPY0
DPolymerase cofactor VP35protein6894% helix, 0% strandQ8JPY0
EPolymerase cofactor VP35protein6295% helix, 0% strandQ8JPY0
FPolymerase cofactor VP35protein6791% helix, 0% strandQ8JPY0
GPolymerase cofactor VP35protein6688% helix, 0% strandQ8JPY0
HPolymerase cofactor VP35protein6394% helix, 0% strandQ8JPY0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14950.640.7750empty

Interfaces

14 interfaces between chains.

  • B–C · 1677 Ų buried · 15 hydrogen bonds · protein-protein
  • A–D · 1631 Ų buried · 18 hydrogen bonds · protein-protein
  • G–H · 1525 Ų buried · 15 hydrogen bonds · protein-protein
  • E–F · 1519 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 1401 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 6GBQ · Crystal Structure of the oligomerization domain of Vp35 from Reston virus · the same entry in another collection · chain A against A, TM-score 1.00

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