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Bile salts alter the mouse norovirus capsid conformation; possible implications for cell attachment and immune evasion.

Analyse Bile salts alter the mouse norovirus capsid conformation; possible implications… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6P4L
Type
protein
Length
601 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid protein
UniProt
Q2V8W4
Pockets
4 · best druggability 0.48

Structure

electron microscopy · 3 distinct chains · 8% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapsid proteinprotein20310% helix, 34% strandQ2V8W4
BCapsid proteinprotein2056% helix, 30% strandQ2V8W4
CCapsid proteinprotein1939% helix, 35% strandQ2V8W4

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11620.480.7729empty
2640.410.8118empty
3850.360.7619empty
4680.300.7416empty

Interfaces

3 interfaces between chains.

  • A–C · 865 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 810 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 805 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 6P4L · Bile salts alter the mouse norovirus capsid conformation; possible implications for cell… · the same entry in another collection · chain A against A, TM-score 1.00

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