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Crystal structure of glutamine synthetase from helicobacter pylori

Analyse Crystal structure of glutamine synthetase from helicobacter pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ZLI
Type
protein
Length
2,846 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamine synthetase
EC
6.3.1.2
UniProt
P94845
Pockets
20 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, FGlutamine synthetase (EC 6.3.1.2)protein47435% helix, 23% strandP94845
B, DGlutamine synthetase (EC 6.3.1.2)protein47535% helix, 24% strandP94845

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19630.800.8273empty
29780.800.8275empty
39380.800.8272empty
410840.790.8069empty
510840.780.7973empty

Interfaces

6 interfaces between chains.

  • A–B · 1963 Ų buried · 42 hydrogen bonds · protein-protein
  • A–F · 1921 Ų buried · 41 hydrogen bonds · protein-protein
  • D–E · 1914 Ų buried · 39 hydrogen bonds · protein-protein
  • E–F · 1901 Ų buried · 38 hydrogen bonds · protein-protein
  • C–D · 1894 Ų buried · 41 hydrogen bonds · protein-protein

Compared structures

  • 5ZLI · Crystal structure of glutamine synthetase from helicobacter pylori · the same entry in another collection · chain F against F, TM-score 1.00
  • P94845 · AlphaFold monomer V2.0 prediction for glutamine synthetase (P94845) · a predicted model of the same protein · chain B against A, TM-score 0.99

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