UniProt T1KUK4
UDP-glycosyltransferase 202A2 (T1KUK4)
UDP-glycosyltransferase 202A2 (UniProt T1KUK4): 7 experimental structures on GenesisL1, 8 ligands bound, 50 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- T1KUK4
- Protein
- UDP-glycosyltransferase 202A2
- Experimental structures
- 7
- Predicted models
- 0
- Ligands
- 8
- Pockets
- 50 · 6 records with a druggable one
Structures
7 records of T1KUK4 in the MolNFT archive: 7 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 6PNT | Structural Characterization of UDP-glycosyltransferase from Tetranychus Urticae | x-ray diffraction | A | — | 3 (best 0.81) |
| 6PNT | Structural characterization of udp-glycosyltransferase from tetranychus urticae | x-ray diffraction | A | — | — |
| 8GKN | Crystal structure of TuUGT202A2 (Tetur22g00270) in complex with S-naringenin | x-ray diffraction | A, B | UDP, NAR | 11 (best 0.83) |
| 8SFT | Crystal structure of TuUGT202A2 (Tetur22g00270) in complex with kaempferol | x-ray diffraction | A, B, C, D | UDP, KMP, SO4, UNL | 20 (best 0.84) |
| 8SFU | Crystal structure of TuUGT202A2 (Tetur22g00270) in complex with naringin | x-ray diffraction | A, B | UDP, ZWN | 10 (best 0.82) |
| 8SFW | Crystal structure of TuUGT202A2 (Tetur22g00270) in complex with quercetin | x-ray diffraction | A | UDP, QUE | 3 (best 0.80) |
| 8SFY | Crystal structure of TuUGT202A2 (Tetur22g00270) in complex with UDP-glucose | x-ray diffraction | A | UPG | 3 (best 0.81) |
Ligands
- UDP · Uridine-5'-diphosphate · in 4 records
- KMP · 3,5,7-trihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one · in 1 record
- NAR · Naringenin · in 1 record
- QUE · 3,5,7,3',4'-pentahydroxyflavone · in 1 record
- SO4 · Sulfate ion · in 1 record
- UNL · Unknown ligand · in 1 record
- UPG · Uridine-5'-diphosphate-glucose · in 1 record
- ZWN · (2S)-5-hydroxy-2-(4-hydroxyphenyl)-4-oxo-3,4-dihydro-2H-1-benzopyran-7-yl 2-O-(6-deoxy-alpha-L-mannopyranosyl)-beta-D-glucopyranoside · in 1 record
Elsewhere
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