MolNFT v1 · #499386 · protein
AlphaFold monomer V2.0 prediction for tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase (B5QVI4)
B5QVI4: “AlphaFold monomer V2.0 prediction for tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase (B5QVI4)”. 2 pockets (best druggability 0.77). MolNFT v1 #499386 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- B5QVI4
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xCe4913b38f6cdd39cE5A2503280B7fe0683920B8
- Molecule
- Tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase
- UniProt
- B5QVI4
- Pockets
- 2 · best druggability 0.77
Structure
1 distinct chain · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tdp-N-ACETYLFUCOSAMINE:LIPID II N-acetylfucosaminyltransferase | protein | 359 | 44% helix, 14% strand | B5QVI4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 767 | 0.77 | 0.81 | 54 | empty |
| 2 | 50 | 0.27 | 0.75 | 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 B5QVI4
- Elsewhere: UniProt B5QVI4 · AlphaFold DB B5QVI4
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