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Cryo-EM structure of mature coxsackievirus A10 at pH 7.4

Analyse Cryo-EM structure of mature coxsackievirus A10 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
7BZN
Type
protein
Length
800 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
14 · best druggability 0.81

Structure

electron microscopy · 4 distinct chains · 8% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapsid protein VP1protein2709% helix, 29% strand—
BCapsid protein VP2protein2468% helix, 26% strandG0YPI2
CCapsid protein VP3protein2406% helix, 30% strandG0YPI2
DCapsid protein VP4protein4414% helix, 7% 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

14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13910.810.9053SPH
2670.730.9825empty
31830.540.7932empty
4840.520.8522empty
51720.510.7825empty

Interfaces

6 interfaces between chains.

  • A–C · 3821 Ų buried · 45 hydrogen bonds · protein-protein
  • A–B · 2275 Ų buried · 35 hydrogen bonds · protein-protein
  • B–C · 1750 Ų buried · 13 hydrogen bonds · protein-protein
  • A–D · 1164 Ų buried · 10 hydrogen bonds · protein-protein
  • C–D · 838 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 7BZN · Cryo-EM structure of mature Coxsackievirus A10 at pH 7.4 · the same entry in another collection · chain A against A, TM-score 1.00

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