Research workbench
AlphaFold monomer V2.0 prediction for disease resistance protein RPM1 (Q39214)
Analyse AlphaFold monomer V2.0 prediction for disease resistance protein RPM1 (Q39214) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q39214
- Type
- protein
- Length
- 926 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Disease resistance protein RPM1
- UniProt
- Q39214
- Pockets
- 9 · best druggability 0.80
Structure
1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disease resistance protein RPM1 | protein | 926 | 42% helix, 16% strand | Q39214 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.80 | 0.81 | 106 | empty |
| 2 | 1156 | 0.76 | 0.78 | 71 | empty |
| 3 | 289 | 0.52 | 0.74 | 41 | empty |
| 4 | 152 | 0.51 | 0.79 | 22 | empty |
| 5 | 244 | 0.50 | 0.75 | 25 | 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 Q39214
- Elsewhere: UniProt Q39214 · AlphaFold DB Q39214
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