MolNFT v1 · #51608 · protein
Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants
2VCH: “Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic…”. X-ray diffraction. MolNFT v1 #51608 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2VCH
- Type
- protein
- Length
- 462 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9M156
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 462 | — | Q9M156 |
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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