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Cryo-EM structure of Murine Norovirus capsid

Analyse Cryo-EM structure of Murine Norovirus capsid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IUK
Type
protein
Length
1,531 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.5
Source
Murine norovirus GV/NIH-2410/2005/USA
Molecule
Major capsid protein VP1
UniProt
B7XA03
Pockets
17 · best druggability 0.76

Structure

electron microscopy · resolution 3.5 · 3 distinct chains · 4% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMajor capsid protein VP1protein5135% helix, 27% strandB7XA03
BMajor capsid protein VP1protein5163% helix, 28% strandB7XA03
CMajor capsid protein VP1protein5025% helix, 28% strandB7XA03

Pockets

17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19880.760.7985empty
24140.760.8564empty
3910.760.9720empty
42630.720.8733empty
53500.600.7745empty

Interfaces

3 interfaces between chains.

  • A–B · 3105 Ų buried · 40 hydrogen bonds · protein-protein
  • B–C · 1945 Ų buried · 25 hydrogen bonds · protein-protein
  • A–C · 1303 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6IUK · Cryo-EM structure of murine norovirus capsid · the same entry in another collection · chain A against A, TM-score 1.00

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