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Alpha-1,2-GLUCOSYLTRANSFERASE_UDP_TLL1591

Analyse Alpha-1,2-GLUCOSYLTRANSFERASE_UDP_TLL1591 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7FG9
Type
protein
Length
682 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycosyl transferase
UniProt
Q8DIJ4
Ligands
UDP
Pockets
3 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGlycosyl transferaseprotein34141% helix, 15% strandQ8DIJ4

Ligands and binding sites

  • UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110130.790.80109UDP
26650.770.8267UDP
3590.410.8115empty

Interfaces

1 interface between chains.

  • A–B · 592 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 7FG9 · Alpha-1,2-glucosyltransferase_UDP_tll1591 · the same entry in another collection · chain A against A, TM-score 1.00

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