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Crystal structure of reston ebolavirus VP35 RNA binding domain

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

PDB
3KS4
Type
protein
Length
249 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polymerase cofactor VP35
UniProt
Q8JPY0
Pockets
1 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolymerase cofactor VP35protein12551% helix, 14% strandQ8JPY0
BPolymerase cofactor VP35protein12452% helix, 14% strandQ8JPY0

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11030.380.7526empty

Interfaces

1 interface between chains.

  • A–B · 496 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 3KS4 · Crystal structure of Reston ebolavirus VP35 RNA binding domain · the same entry in another collection · chain A against A, TM-score 1.00

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