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Cryo-EM structure of mature coxsackievirus A10 at pH 5.5

Analyse Cryo-EM structure of mature coxsackievirus A10 at pH 5.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7BZO
Type
protein
Length
793 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
UniProt
G0YPI2
Ligands
SPH
Pockets
10 · best druggability 0.81

Structure

electron microscopy · 4 distinct chains · 9% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapsid protein VP1protein2718% helix, 28% strand—
BCapsid protein VP2protein24611% helix, 28% strandG0YPI2
CCapsid protein VP3protein2398% helix, 30% strandG0YPI2
DCapsid protein VP4protein3716% helix, 8% strandG0YPI2

Ligands and binding sites

  • SPH · Sphingosine · ligand · chains A, C

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

Pockets

10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13610.810.9044SPH
22670.580.7940empty
3810.450.8112empty
41060.450.7816empty
5680.400.8017empty

Interfaces

6 interfaces between chains.

  • A–C · 3809 Ų buried · 49 hydrogen bonds · protein-protein
  • A–B · 2291 Ų buried · 35 hydrogen bonds · protein-protein
  • B–C · 1696 Ų buried · 13 hydrogen bonds · protein-protein
  • A–D · 1088 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 773 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 7BZO · Cryo-EM structure of mature Coxsackievirus A10 at pH 5.5 · the same entry in another collection · chain A against A, TM-score 1.00

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