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Structure of Helicobacter pylori EgtU bound to EGT

Analyse Structure of Helicobacter pylori EgtU bound to EGT in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
8DP7
Type
protein
Length
1,325 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.35
Source
Helicobacter pylori (strain P12)
Molecule
Osmoprotection protein
UniProt
B6JM49
Ligands
LW8
Pockets
12 · best druggability 0.77

Structure

x-ray diffraction · resolution 3.35 · 1 distinct chain · 49% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EOsmoprotection proteinprotein26549% helix, 18% strandB6JM49

Ligands and binding sites

  • LW8 · trimethyl-[(2S)-1-oxidanyl-1-oxidanylidene-3-(2-sulfanylidene-1,3-dihydroimidazol-4-yl)propan-2-yl]azanium · ligand · 5 copies · chains A, B, C, D, E

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

Pockets

12 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12630.770.8936LW8
26320.760.8270LW8
32310.750.8934LW8
42480.740.8837LW8
58650.730.7876empty

Interfaces

5 interfaces between chains.

  • A–E · 590 Ų buried · 5 hydrogen bonds · protein-protein
  • D–E · 590 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 520 Ų buried · 5 hydrogen bonds · protein-protein
  • C–E · 438 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 390 Ų buried · 3 hydrogen bonds · protein-protein

Analyse

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