Research workbench
AlphaFold monomer V2.0 prediction for sigma-E factor regulatory protein rseb (P0AFY1)
Analyse AlphaFold monomer V2.0 prediction for sigma-E factor regulatory protein rseb… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0AFY1
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Sigma-E factor regulatory protein rseb
- UniProt
- P0AFY1
- Pockets
- 4 · best druggability 0.54
Structure
1 distinct chain · 12% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sigma-E factor regulatory protein rseb | protein | 318 | 12% helix, 46% strand | P0AFY1 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 208 | 0.54 | 0.78 | 33 | empty |
| 2 | 148 | 0.38 | 0.73 | 29 | empty |
| 3 | 73 | 0.31 | 0.74 | 12 | empty |
| 4 | 59 | 0.27 | 0.73 | 15 | 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 P0AFY1
- Elsewhere: UniProt P0AFY1 · AlphaFold DB P0AFY1
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