Research workbench
AlphaFold monomer V2.0 prediction for tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase (A9MXG5)
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
- A9MXG5
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase
- UniProt
- A9MXG5
- Pockets
- 3 · best druggability 0.74
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 | A9MXG5 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 644 | 0.74 | 0.81 | 52 | empty |
| 2 | 53 | 0.48 | 0.86 | 16 | empty |
| 3 | 70 | 0.29 | 0.73 | 12 | 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 A9MXG5
- Elsewhere: UniProt A9MXG5 · AlphaFold DB A9MXG5
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