Research workbench
AlphaFold monomer V2.0 prediction for flagellar P-ring protein 2 (Q2SDU5)
Analyse AlphaFold monomer V2.0 prediction for flagellar P-ring protein 2 (Q2SDU5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2SDU5
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF3b04d65F1aD0058771B149FB8BD62b3934a8918
- Molecule
- Flagellar P-ring protein 2
- UniProt
- Q2SDU5
- Pockets
- 1 · best druggability 0.35
Structure
1 distinct chain · 23% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar P-ring protein 2 | protein | 378 | 23% helix, 31% strand | Q2SDU5 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.35 | 0.76 | 13 | 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 Q2SDU5
- Elsewhere: UniProt Q2SDU5 · AlphaFold DB Q2SDU5
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