Research workbench
AlphaFold monomer V2.0 prediction for tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase (Q0TAT1)
Analyse AlphaFold monomer V2.0 prediction for tdp-N-ACETYLFUCOSAMINE:LIPID II… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0TAT1
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC8EC2E6D757E959bb64e7BAd42bEe5eFaAd0809D
- Molecule
- Tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase
- UniProt
- Q0TAT1
- Pockets
- 1 · best druggability 0.78
Structure
1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase | protein | 359 | 45% helix, 14% strand | Q0TAT1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 818 | 0.78 | 0.81 | 60 | empty |
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 Q0TAT1
- Elsewhere: UniProt Q0TAT1 · AlphaFold DB Q0TAT1
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