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Glutamine binding protein open ligand-free structure

Analyse Glutamine binding protein open ligand-free structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GGG
Type
protein
Length
440 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamine binding protein
UniProt
P10344
Pockets
3 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGlutamine binding proteinprotein22036% helix, 28% strandP10344

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1830.350.7515empty
2920.330.7420empty
3800.310.7321empty

Interfaces

1 interface between chains.

  • A–B · 565 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 1GGG · Glutamine binding protein open ligand-free structure · the same entry in another collection · chain A against A, TM-score 1.00

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