Research workbench
AlphaFold monomer V2.0 prediction for flagellar P-ring protein (O67608)
Analyse AlphaFold monomer V2.0 prediction for flagellar P-ring protein (O67608) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O67608
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9A56922FbaEc811f803d391e4C6E0a6e08B2a5F0
- Molecule
- Flagellar P-ring protein
- UniProt
- O67608
- Pockets
- 2 · best druggability 0.46
Structure
1 distinct chain · 19% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar P-ring protein | protein | 360 | 19% helix, 36% strand | O67608 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.46 | 0.83 | 13 | empty |
| 2 | 56 | 0.31 | 0.76 | 16 | 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 O67608
- Elsewhere: UniProt O67608 · AlphaFold DB O67608
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