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Structure of cagx from a cryo-EM reconstruction of a T4SS

Analyse Structure of cagx from a cryo-EM reconstruction of a T4SS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6OEG
Type
protein
Length
2,268 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Type IV secretion system apparatus protein cagx
UniProt
A0A2J9KJM4
Pockets
20 · best druggability 0.62

Structure

electron microscopy · 1 distinct chain · 23% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
N, O, P, Q, R, S, T, U, V, W, X, Y, Z, aType IV secretion system apparatus protein cagxprotein16223% helix, 23% strandA0A2J9KJM4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14110.620.7747empty
23490.580.7633empty
33170.570.7637empty
43700.570.7539empty
53220.560.7635empty

Interfaces

14 interfaces between chains.

  • R–S · 518 Ų buried · 3 hydrogen bonds · protein-protein
  • V–W · 461 Ų buried · 2 hydrogen bonds · protein-protein
  • X–Y · 456 Ų buried · 2 hydrogen bonds · protein-protein
  • V–a · 450 Ų buried · 2 hydrogen bonds · protein-protein
  • N–a · 450 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 6OEG · Structure of CagX from a cryo-EM reconstruction of a T4SS · the same entry in another collection · chain N against N, TM-score 1.00

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