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MolNFT v1 · #51734 · protein

Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants

2VG8 · Hydroquinone glucosyltransferase: “Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic…”. X-ray diffraction, 1 ligand (UDP), 6 pockets (best druggability 0.81). MolNFT v1 #51734…

PDB
2VG8
Type
protein
Length
465 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hydroquinone glucosyltransferase
EC
2.4.1.218
UniProt
Q9M156
Ligands
UDP
Pockets
6 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHydroquinone glucosyltransferase (EC 2.4.1.218)protein46545% helix, 13% strandQ9M156

Ligands and binding sites

  • UDP · Uridine-5'-diphosphate · ligand · chains A
  • EDO · 1,2-ethanediol · additive · 9 copies · chains A
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13950.810.8957UDP, TRS, EDO
21760.620.8331EDO
31490.480.7722empty
41860.470.7523EDO
5960.360.7418empty

Compared structures

  • 2VG8 · Characterization and engineering of the bifunctional N- and O- glucosyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9M156 · AlphaFold monomer V2.0 prediction for udp-glycosyltransferase 72B1 (Q9M156) · a predicted model of the same protein · chain A against A, TM-score 0.99

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