Research workbench
Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants
Analyse Characterization and engineering of the bifunctional N- and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VCH
- Type
- protein
- Length
- 462 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
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroquinone glucosyltransferase (EC 2.4.1.218) | protein | 462 | 46% helix, 13% strand | Q9M156 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · chains A
- EDO · 1,2-ethanediol · additive · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 397 | 0.79 | 0.88 | 56 | UDP, EDO |
| 2 | 202 | 0.58 | 0.80 | 30 | empty |
| 3 | 179 | 0.47 | 0.75 | 22 | EDO |
| 4 | 135 | 0.46 | 0.77 | 22 | empty |
| 5 | 72 | 0.33 | 0.75 | 14 | empty |
Compared structures
- 2VCH · 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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9M156
- Elsewhere: RCSB PDB 2VCH · PDBe 2VCH · UniProt Q9M156
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