Research workbench
AlphaFold monomer V2.0 prediction for lipopolysaccharide 1,2-N-acetylglucosaminetransferase (P27242)
Analyse AlphaFold monomer V2.0 prediction for lipopolysaccharide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P27242
- Type
- protein
- Length
- 357 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xaC7B45343fbE25Fa32F5775ED488B4BE2cFC14AB
- Molecule
- Lipopolysaccharide 1,2-N-acetylglucosaminetransferase
- UniProt
- P27242
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipopolysaccharide 1,2-N-acetylglucosaminetransferase | protein | 357 | 47% helix, 15% strand | P27242 |
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 | 537 | 0.69 | 0.79 | 50 | empty |
| 2 | 129 | 0.40 | 0.75 | 21 | 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 P27242
- Elsewhere: UniProt P27242 · AlphaFold DB P27242
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