Research workbench
AlphaFold monomer V2.0 prediction for N-acetylglucosaminyltransferase (P04341)
Analyse AlphaFold monomer V2.0 prediction for N-acetylglucosaminyltransferase (P04341) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P04341
- Type
- protein
- Length
- 426 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9073C46348542FfE4327c3F363F9B51B22058e75
- Molecule
- N-acetylglucosaminyltransferase
- UniProt
- P04341
- Pockets
- 5 · best druggability 0.84
Structure
1 distinct chain · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylglucosaminyltransferase | protein | 426 | 51% helix, 13% strand | P04341 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1147 | 0.84 | 0.85 | 88 | empty |
| 2 | 138 | 0.42 | 0.75 | 16 | empty |
| 3 | 86 | 0.41 | 0.77 | 16 | empty |
| 4 | 97 | 0.37 | 0.75 | 17 | empty |
| 5 | 63 | 0.28 | 0.74 | 18 | 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 P04341
- Elsewhere: UniProt P04341 · AlphaFold DB P04341
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