Research workbench
AlphaFold monomer V2.0 prediction for disease resistance protein RGA5 (Q2R8L1)
Analyse AlphaFold monomer V2.0 prediction for disease resistance protein RGA5 (Q2R8L1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2R8L1
- Type
- protein
- Length
- 1,301 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- Molecule
- Disease resistance protein RGA5
- UniProt
- Q2R8L1
- Pockets
- 17 · best druggability 0.84
Structure
1 distinct chain · 38% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disease resistance protein RGA5 | protein | 1301 | 38% helix, 14% strand | Q2R8L1 |
Pockets
17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.84 | 0.85 | 96 | empty |
| 2 | 681 | 0.77 | 0.82 | 54 | empty |
| 3 | 647 | 0.70 | 0.78 | 61 | empty |
| 4 | 273 | 0.68 | 0.83 | 34 | empty |
| 5 | 464 | 0.68 | 0.79 | 49 | 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 Q2R8L1
- Elsewhere: UniProt Q2R8L1 · AlphaFold DB Q2R8L1
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