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Cryo-EM structure of helicobacter pylori vaca hexamer

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

PDB
6ODY
Type
protein
Length
4,158 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Vacuolating cytotoxin autotransporter
UniProt
Q48245
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 4% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FVacuolating cytotoxin autotransporterprotein6934% helix, 27% strandQ48245

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110400.860.88142empty
211280.860.88136empty
310590.860.88139empty
49870.860.87136empty
511490.860.87136empty

Interfaces

6 interfaces between chains.

  • B–C · 421 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 419 Ų buried · 3 hydrogen bonds · protein-protein
  • D–E · 418 Ų buried · 3 hydrogen bonds · protein-protein
  • A–F · 417 Ų buried · 3 hydrogen bonds · protein-protein
  • E–F · 417 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 6ODY · Cryo-EM structure of Helicobacter pylori VacA hexamer · the same entry in another collection · chain C against C, TM-score 1.00
  • Q48245 · AlphaFold monomer V2.0 prediction for vacuolating cytotoxin autotransporter (Q48245) · a predicted model of the same protein · chain A against A, TM-score 0.96

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