Research workbench
AlphaFold monomer V2.0 prediction for lipopolysaccharide core biosynthesis protein rfas (P27126)
Analyse AlphaFold monomer V2.0 prediction for lipopolysaccharide core biosynthesis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P27126
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Lipopolysaccharide core biosynthesis protein rfas
- UniProt
- P27126
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipopolysaccharide core biosynthesis protein rfas | protein | 311 | 35% helix, 17% strand | P27126 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 390 | 0.67 | 0.80 | 34 | empty |
| 2 | 149 | 0.41 | 0.74 | 30 | empty |
| 3 | 57 | 0.33 | 0.77 | 12 | 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 P27126
- Elsewhere: UniProt P27126 · AlphaFold DB P27126
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