UniProt D3T4E0
N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase (D3T4E0)
N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase (UniProt D3T4E0), EC 2.4.1.187: 8 experimental structures on GenesisL1, 4 ligands bound, 29 pockets. Binding sites, pockets, druggability and 3D…
- UniProt
- D3T4E0
- Protein
- N-acetylglucosaminyldiphosphoundecaprenol…
- EC
- 2.4.1.187
- Experimental structures
- 8
- Predicted models
- 0
- Ligands
- 4
- Pockets
- 29 · 3 records with a druggable one
Structures
8 records of D3T4E0 in the MolNFT archive: 8 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 5WB4 | Crystal structure of the TarA wall teichoic acid glycosyltransferase | x-ray diffraction | A, B, C, D, E, F, G, H | SO4 | 16 (best 0.85) |
| 5WB4 | Crystal structure of the tara wall teichoic acid glycosyltransferase | x-ray diffraction | A, B, C, D, E, F, G, H | SO4 | — |
| 5WFG | Crystal structure of the TarA wall teichoic acid glycosyltransferase bound to UDP | x-ray diffraction | A, B, C, D, E, F | UDP | 7 (best 0.80) |
| 5WFG | Crystal structure of the tara wall teichoic acid glycosyltransferase bound to udp | x-ray diffraction | A, B, C, D, E, F | UDP | — |
| 7MPK | Crystal structure of TagA with UDP-GlcNAc | x-ray diffraction | A, B, C | UD1 | — |
| 7MPK | Crystal structure of taga with udp-glcnac | x-ray diffraction | A, B, C | UD1 | — |
| 7N41 | Crystal structure of TagA with UDP-ManNAc | x-ray diffraction | A, B, C | UD9 | 6 (best 0.83) |
| 7N41 | Crystal structure of taga with udp-mannac | x-ray diffraction | A, B, C | UD9 | — |
Ligands
- SO4 · Sulfate ion · in 2 records
- UD1 · Uridine-diphosphate-N-acetylglucosamine · in 2 records
- UD9 · (2R,3S,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxyoxolan-2-yl]methyl dihydrogen diphosphate (non-preferred name) · in 2 records
- UDP · Uridine-5'-diphosphate · in 2 records
Elsewhere
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