Research workbench
AlphaFold monomer V2.0 prediction for N-acetylglucosaminyltransferase (P24151)
Analyse AlphaFold monomer V2.0 prediction for N-acetylglucosaminyltransferase (P24151) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P24151
- Type
- protein
- Length
- 428 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2b47CE81494c5321B3929F4cE4EA361c06Eba2E2
- Molecule
- N-acetylglucosaminyltransferase
- UniProt
- P24151
- Pockets
- 3 · best druggability 0.88
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylglucosaminyltransferase | protein | 428 | 52% helix, 12% strand | P24151 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1182 | 0.88 | 0.90 | 124 | empty |
| 2 | 401 | 0.61 | 0.76 | 40 | empty |
| 3 | 156 | 0.49 | 0.77 | 20 | 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 P24151
- Elsewhere: UniProt P24151 · AlphaFold DB P24151
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