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Atomic structure of the Epstein-Barr portal, structure II

Analyse Atomic structure of the Epstein-Barr portal, structure II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6RVS
Type
protein
Length
4,764 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.59
Source
Epstein-Barr virus (strain GD1)
Molecule
Portal protein
UniProt
A0A0B6VPI0
Pockets
20 · best druggability 0.81

Structure

electron microscopy · resolution 3.59 · 1 distinct chain · 50% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LPortal proteinprotein39750% helix, 13% strandA0A0B6VPI0

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19270.810.8383empty
29370.810.8383empty
38950.810.8381empty
49210.810.8383empty
58700.810.8376empty

Interfaces

24 interfaces between chains.

  • H–I · 3994 Ų buried · 27 hydrogen bonds · protein-protein
  • G–H · 3993 Ų buried · 27 hydrogen bonds · protein-protein
  • I–J · 3987 Ų buried · 27 hydrogen bonds · protein-protein
  • D–E · 3986 Ų buried · 27 hydrogen bonds · protein-protein
  • F–G · 3985 Ų buried · 27 hydrogen bonds · protein-protein

Compared structures

  • 6RVS · Atomic structure of the epstein-barr portal, structure II · the same entry in another collection · chain A against A, TM-score 1.00

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