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Alpha-,1,3 galactosyltransferase - alpha-D-glucose complex

Analyse Alpha-,1,3 galactosyltransferase - alpha-D-glucose complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GWW
Type
protein
Length
574 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-acetyllactosaminide alpha-1,3-galactosyltransferase
EC
2.4.1.151
UniProt
P14769
Ligands
UDP, GLC, MN
Pockets
5 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BN-acetyllactosaminide alpha-1,3-galactosyltransferase (EC 2.4.1.151)protein28737% helix, 20% strandP14769

Ligands and binding sites

  • UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, B
  • GLC · alpha-D-glucopyranose · sugar · chains B
  • MN · Manganese (II) ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13430.750.8644UDP, MN, GLC
22930.730.8633UDP, MN
32070.620.8237empty
41020.380.7521empty
5650.280.7314empty

Interfaces

1 interface between chains.

  • A–B · 827 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 1GWW · Alpha-,1,3 galactosyltransferase - alpha-D-glucose complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P14769 · AlphaFold monomer V2.0 prediction for N-acetyllactosaminide… · a predicted model of the same protein · chain B against A, TM-score 1.00

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