Research workbench
AlphaFold monomer V2.0 prediction for ecf RNA polymerase sigma-E factor (P0AGB8)
Analyse AlphaFold monomer V2.0 prediction for ecf RNA polymerase sigma-E factor (P0AGB8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0AGB8
- Type
- protein
- Length
- 191 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- Ecf RNA polymerase sigma-E factor
- UniProt
- P0AGB8
- Pockets
- 3 · best druggability 0.46
Structure
1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ecf RNA polymerase sigma-E factor | protein | 191 | 68% helix, 0% strand | P0AGB8 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.46 | 0.74 | 26 | empty |
| 2 | 70 | 0.36 | 0.77 | 19 | empty |
| 3 | 69 | 0.32 | 0.74 | 11 | 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 P0AGB8
- Elsewhere: UniProt P0AGB8 · AlphaFold DB P0AGB8
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