Research workbench
AlphaFold monomer V2.0 prediction for tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase (B5BIU1)
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
- B5BIU1
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- Tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase
- UniProt
- B5BIU1
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase | protein | 359 | 46% helix, 14% strand | B5BIU1 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 612 | 0.76 | 0.82 | 40 | empty |
| 2 | 60 | 0.51 | 0.86 | 18 | empty |
| 3 | 129 | 0.42 | 0.76 | 18 | empty |
| 4 | 54 | 0.27 | 0.74 | 13 | 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 B5BIU1
- Elsewhere: UniProt B5BIU1 · AlphaFold DB B5BIU1
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