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Structure of ESPG3 chaperone from the type VII (esx-3) secretion system

Analyse Structure of ESPG3 chaperone from the type VII (esx-3) secretion system in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4L4W
Type
protein
Length
529 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ESPG3
UniProt
A0QQ45
Pockets
5 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AESPG3protein26236% helix, 31% strandA0QQ45
BESPG3protein26735% helix, 30% strandA0QQ45

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15750.760.8376empty
22580.630.8129empty
32570.610.8026empty
4830.370.7621empty
5610.300.7515empty

Interfaces

1 interface between chains.

  • A–B · 999 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

  • 4L4W · Structure of EspG3 chaperone from the type VII (ESX-3) secretion system · the same entry in another collection · chain A against A, TM-score 1.00
  • A0QQ45 · AlphaFold monomer V2.0 prediction for esx-3 secretion-associated protein ESPG3 (A0QQ45) · a predicted model of the same protein · chain A against A, TM-score 0.96

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