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Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic TRANSPORT(SLASH)CHEMOTACTIC protein receptor for D- glucose and D-galactose

Analyse Crystallographic analysis of the epimeric and anomeric specificity of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GLG
Type
protein
Length
309 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GALACTOSE/GLUCOSE-binding protein
UniProt
P02927
Ligands
GAL, CA
Pockets
1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGALACTOSE/GLUCOSE-binding proteinprotein30943% helix, 19% strandP02927

Ligands and binding sites

  • GAL · beta-D-galactopyranose · sugar · chains A
  • CA · Calcium ion · metal · chains A

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
1600.340.7614empty

Compared structures

  • 1GLG · Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic… · the same entry in another collection · chain A against A, TM-score 1.00

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