GL1X · GenesisL1 explorer

MolNFT v1 · #138795 · protein

Crystal structure of flif-flig complex from H. pylori

5WUJ · Flagellar M-ring protein: “Crystal structure of flif-flig complex from H. pylori”. X-ray diffraction, 1 pocket (best druggability 0.31). MolNFT v1 #138795 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
5WUJ
Type
protein
Length
142 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Flagellar M-ring protein; Flagellar motor switch protein flig
UniProt
O25118, O25119
Pockets
1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFlagellar M-ring proteinprotein3789% helix, 0% strandO25118
BFlagellar motor switch protein fligprotein10579% helix, 0% strandO25119

Ligands and binding sites

  • GOL · Glycerol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1800.310.7317empty

Interfaces

1 interface between chains.

  • A–B · 1469 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 5WUJ · Crystal structure of FliF-FliG complex from H. pylori · the same entry in another collection · chain A against A, TM-score 1.00
  • O25119 · AlphaFold monomer V2.0 prediction for flagellar motor switch protein flig (O25119) · a predicted model of the same protein · chain B against A, TM-score 0.66

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