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Structure of ebola virus nucleoprotein N-terminal fragment bound to a peptide derived from ebola VP35

Analyse Structure of ebola virus nucleoprotein N-terminal fragment bound to a peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4YPI
Type
protein
Length
1,500 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nucleoprotein; Polymerase cofactor VP35
UniProt
P18272, Q05127
Pockets
13 · best druggability 0.79

Structure

x-ray diffraction · 4 distinct chains · 66% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CNucleoproteinprotein34867% helix, 6% strandP18272
G, E, F, HPolymerase cofactor VP35protein2839% helix, 4% strandQ05127
ANucleoproteinprotein34666% helix, 6% strandP18272
B, DNucleoproteinprotein34767% helix, 6% strandP18272

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19780.790.81116empty
23380.670.8137empty
3600.530.8715empty
4680.410.8020empty
5920.410.7720empty

Interfaces

17 interfaces between chains.

  • B–F · 1365 Ų buried · 17 hydrogen bonds · protein-protein
  • C–G · 1344 Ų buried · 19 hydrogen bonds · protein-protein
  • D–H · 1331 Ų buried · 14 hydrogen bonds · protein-protein
  • A–E · 1321 Ų buried · 12 hydrogen bonds · protein-protein
  • C–A · 797 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 4YPI · Structure of Ebola virus nucleoprotein N-terminal fragment bound to a peptide derived… · the same entry in another collection · chain C against C, TM-score 1.00

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