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Norovirus T=3 GII.4 hov vlp

Analyse Norovirus T=3 GII.4 hov vlp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7MRY
Type
protein
Length
1,460 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
VP1
UniProt
A9YYE4
Pockets
15 · best druggability 0.74

Structure

electron microscopy · 2 distinct chains · 7% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVP1protein4887% helix, 32% strandA9YYE4
B, CVP1protein4867% helix, 36% strandA9YYE4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15500.740.8251empty
25500.720.8060empty
34260.670.8058empty
42870.560.7735empty
5950.510.8320empty

Interfaces

3 interfaces between chains.

  • A–C · 835 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 760 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 754 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 7MRY · Norovirus T=3 GII.4 HOV VLP · the same entry in another collection · chain A against A, TM-score 1.00

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