Research workbench
AlphaFold monomer V2.0 prediction for beta-1,3-N-acetylglucosaminyltransferase radical fringe (Q6KFX9)
Analyse AlphaFold monomer V2.0 prediction for beta-1,3-N-acetylglucosaminyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6KFX9
- Type
- protein
- Length
- 362 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Beta-1,3-N-acetylglucosaminyltransferase radical fringe
- UniProt
- Q6KFX9
- Pockets
- 2 · best druggability 0.54
Structure
1 distinct chain · 40% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-1,3-N-acetylglucosaminyltransferase radical fringe | protein | 362 | 40% helix, 13% strand | Q6KFX9 |
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 | 202 | 0.54 | 0.79 | 27 | empty |
| 2 | 85 | 0.33 | 0.74 | 11 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 Q6KFX9
- Elsewhere: UniProt Q6KFX9 · AlphaFold DB Q6KFX9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.