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Cryo-EM structure of full echovirus 11 particle at pH 7.4

Analyse Cryo-EM structure of full echovirus 11 particle at pH 7.4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LA3
Type
protein
Length
833 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid protein VP1; Capsid protein VP2; Capsid protein VP3; Capsid protein VP4
Ligands
SPH
Pockets
13 · best druggability 0.80

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapsid protein VP1protein28510% helix, 34% strand—
BCapsid protein VP2protein2519% helix, 37% strand—
CCapsid protein VP3protein2388% helix, 29% 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, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15970.800.8572SPH
2570.710.9821empty
31850.520.7828empty
41060.500.8222empty
51000.430.7813empty

Interfaces

6 interfaces between chains.

  • A–C · 4389 Ų buried · 59 hydrogen bonds · protein-protein
  • A–B · 2048 Ų buried · 25 hydrogen bonds · protein-protein
  • B–C · 1549 Ų buried · 15 hydrogen bonds · protein-protein
  • A–D · 1500 Ų buried · 21 hydrogen bonds · protein-protein
  • C–D · 922 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6LA3 · Cryo-EM structure of full echovirus 11 particle at pH 7.4 · the same entry in another collection · chain A against A, TM-score 1.00

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