Research workbench
AlphaFold monomer V2.0 prediction for tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase (B5EZ52)
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
- B5EZ52
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase
- UniProt
- B5EZ52
- Pockets
- 1 · best druggability 0.76
Structure
1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase | protein | 359 | 45% helix, 15% strand | B5EZ52 |
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 | 708 | 0.76 | 0.81 | 65 | 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 B5EZ52
- Elsewhere: UniProt B5EZ52 · AlphaFold DB B5EZ52
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