Research workbench
AlphaFold monomer V2.0 prediction for secreted rxlr effector protein 27 (A0A172M468)
Analyse AlphaFold monomer V2.0 prediction for secreted rxlr effector protein 27… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A172M468
- Type
- protein
- Length
- 235 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Secreted rxlr effector protein 27
- Pockets
- 3 · best druggability 0.79
Structure
1 distinct chain · 62% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Secreted rxlr effector protein 27 | protein | 235 | 62% helix, 9% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 402 | 0.79 | 0.87 | 39 | empty |
| 2 | 260 | 0.58 | 0.78 | 26 | empty |
| 3 | 58 | 0.29 | 0.74 | 13 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
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