Research workbench
AlphaFold monomer V2.0 prediction for beta-1,3-N-acetylglucosaminyltransferase radical fringe (O12972)
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
- O12972
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xCcE0f7d4E847A12eE8F3c53aeE79dC9c9B1cB849
- Molecule
- Beta-1,3-N-acetylglucosaminyltransferase radical fringe
- UniProt
- O12972
- Pockets
- 2 · best druggability 0.57
Structure
1 distinct chain · 34% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-1,3-N-acetylglucosaminyltransferase radical fringe | protein | 372 | 34% helix, 14% strand | O12972 |
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 | 192 | 0.57 | 0.80 | 28 | empty |
| 2 | 58 | 0.29 | 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 O12972
- Elsewhere: UniProt O12972 · AlphaFold DB O12972
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