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Mouse norovirus protruding domain complexed with neutralizing Fab fragment from mab A6.2

Analyse Mouse norovirus protruding domain complexed with neutralizing Fab fragment from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7L5J
Type
protein
Length
1,469 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid protein; Anti mouse norovirus mab A6.2 Fab light chain; Anti mouse norovirus mab…
UniProt
Q2V8W4
Pockets
19 · best druggability 0.85

Structure

electron microscopy · 4 distinct chains · 4% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapsid proteinprotein3054% helix, 22% strandQ2V8W4
BCapsid proteinprotein3044% helix, 24% strandQ2V8W4
L, XAnti mouse norovirus mab A6.2 Fab light chainprotein2105% helix, 37% strand—
W, YAnti mouse norovirus mab A6.2 Fab heavy chainprotein2201% helix, 45% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16670.850.8978empty
26270.650.7551empty
3680.580.8923empty
44220.570.7471empty
54330.550.7343empty

Interfaces

8 interfaces between chains.

  • L–W · 2006 Ų buried · 14 hydrogen bonds · protein-protein
  • X–Y · 1935 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 1890 Ų buried · 13 hydrogen bonds · protein-protein
  • A–Y · 711 Ų buried · 4 hydrogen bonds · protein-protein
  • B–W · 677 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 7L5J · Mouse Norovirus Protruding domain complexed with neutralizing Fab fragment from mAb A6.2 · the same entry in another collection · chain A against A, TM-score 1.00

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