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Cryo-EM structure of echovirus 11 complexed with its attaching receptor CD55 at pH 5.5

Analyse Cryo-EM structure of echovirus 11 complexed with its attaching receptor CD55 at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LAO
Type
protein
Length
833 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.64
Source
Echovirus E11
Molecule
Capsid protein VP1; Capsid protein VP2; Capsid protein VP3; Capsid protein VP4
Ligands
SPH
Pockets
13 · best druggability 0.78

Structure

electron microscopy · resolution 2.64 · 4 distinct chains · 9% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapsid protein VP1protein2859% helix, 32% strand—
BCapsid protein VP2protein25110% helix, 38% strand—
CCapsid protein VP3protein2388% helix, 30% strand—
DCapsid protein VP4protein5912% helix, 17% strand—

Ligands and binding sites

  • SPH · Sphingosine · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16020.780.8483SPH
2500.700.9816empty
3780.530.8628empty
41290.520.8130empty
51780.510.7828empty

Interfaces

6 interfaces between chains.

  • A–C · 4470 Ų buried · 57 hydrogen bonds · protein-protein
  • A–B · 2100 Ų buried · 25 hydrogen bonds · protein-protein
  • B–C · 1553 Ų buried · 14 hydrogen bonds · protein-protein
  • A–D · 1485 Ų buried · 18 hydrogen bonds · protein-protein
  • C–D · 924 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6LAO · Cryo-EM structure of echovirus 11 complexed with its attaching receptor CD55 at pH 5.5 · the same entry in another collection · chain A against A, TM-score 1.00

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