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Crystal structure of EVP30 C-terminus and enp peptide

Analyse Crystal structure of EVP30 C-terminus and enp peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5VAP
Type
protein
Length
246 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Minor nucleoprotein VP30; Np
UniProt
Q77DJ5, A0A0D5W865
Pockets
1 · best druggability 0.68

Structure

x-ray diffraction · 4 distinct chains · 66% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMinor nucleoprotein VP30protein11173% helix, 0% strandQ77DJ5
DNpprotein120% helix, 0% strandA0A0D5W865
BMinor nucleoprotein VP30protein11272% helix, 0% strandQ77DJ5
CNpprotein110% helix, 0% strandA0A0D5W865

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12710.680.8437empty

Interfaces

4 interfaces between chains.

  • B–C · 644 Ų buried · 8 hydrogen bonds · protein-protein
  • A–D · 631 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 464 Ų buried · 6 hydrogen bonds · protein-protein
  • D–B · 60 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5VAP · Crystal structure of eVP30 C-terminus and eNP peptide · the same entry in another collection · chain A against A, TM-score 1.00

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