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Cryo-EM structure for hepatitis a virus complexed with Fab

Analyse Cryo-EM structure for hepatitis a virus complexed with Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5WTH
Type
protein
Length
1,152 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polyprotein; VP2; VP3; Fab light chain; Fab heavy chain
Pockets
14 · best druggability 0.71

Structure

electron microscopy · 5 distinct chains · 8% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolyproteinprotein26012% helix, 28% strand—
BVP2protein2179% helix, 39% strand—
CVP3protein2469% helix, 31% strand—
DFab light chainprotein2126% helix, 47% strand—
EFab heavy chainprotein2174% helix, 53% strand—

Pockets

14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14990.710.8163empty
24260.650.7850empty
34520.610.7649empty
41920.460.7533empty
51310.440.7623empty

Interfaces

6 interfaces between chains.

  • A–C · 3830 Ų buried · 51 hydrogen bonds · protein-protein
  • D–E · 1984 Ų buried · 18 hydrogen bonds · protein-protein
  • B–C · 1466 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 1370 Ų buried · 15 hydrogen bonds · protein-protein
  • B–D · 266 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 5WTH · Cryo-EM structure for Hepatitis A virus complexed with FAB · the same entry in another collection · chain A against A, TM-score 1.00

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