Research workbench
AlphaFold monomer V2.0 prediction for secreted rxlr effector protein 111 (P0CV44)
Analyse AlphaFold monomer V2.0 prediction for secreted rxlr effector protein 111… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CV44
- Type
- protein
- Length
- 451 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x380994D123977e35e4705A8d85Ebc8F421A9D395
- Molecule
- Secreted rxlr effector protein 111
- UniProt
- P0CV44
- Pockets
- 7 · best druggability 0.67
Structure
1 distinct chain · 50% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Secreted rxlr effector protein 111 | protein | 451 | 50% helix, 0% strand | P0CV44 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 566 | 0.67 | 0.77 | 49 | empty |
| 2 | 72 | 0.42 | 0.80 | 13 | empty |
| 3 | 125 | 0.39 | 0.74 | 23 | empty |
| 4 | 85 | 0.39 | 0.77 | 13 | empty |
| 5 | 64 | 0.37 | 0.78 | 12 | 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 P0CV44
- Elsewhere: UniProt P0CV44 · AlphaFold DB P0CV44
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