Research workbench
AlphaFold monomer V2.0 prediction for secreted rxlr effector protein 108 (P0CV43)
Analyse AlphaFold monomer V2.0 prediction for secreted rxlr effector protein 108… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CV43
- Type
- protein
- Length
- 510 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- Secreted rxlr effector protein 108
- UniProt
- P0CV43
- Pockets
- 5 · best druggability 0.75
Structure
1 distinct chain · 46% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Secreted rxlr effector protein 108 | protein | 510 | 46% helix, 0% strand | P0CV43 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 869 | 0.75 | 0.79 | 89 | empty |
| 2 | 181 | 0.55 | 0.79 | 28 | empty |
| 3 | 100 | 0.40 | 0.76 | 16 | empty |
| 4 | 66 | 0.35 | 0.77 | 15 | empty |
| 5 | 75 | 0.31 | 0.73 | 14 | 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 P0CV43
- Elsewhere: UniProt P0CV43 · AlphaFold DB P0CV43
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