Research workbench
AlphaFold monomer V2.0 prediction for RAD52 motif-containing protein 1 (Q4R856)
Analyse AlphaFold monomer V2.0 prediction for RAD52 motif-containing protein 1 (Q4R856) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4R856
- Type
- protein
- Length
- 284 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
- Molecule
- RAD52 motif-containing protein 1
- UniProt
- Q4R856
- Pockets
- 5 · best druggability 0.62
Structure
1 distinct chain · 25% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAD52 motif-containing protein 1 | protein | 284 | 25% helix, 27% strand | Q4R856 |
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 | 483 | 0.62 | 0.75 | 43 | empty |
| 2 | 454 | 0.58 | 0.74 | 41 | empty |
| 3 | 74 | 0.34 | 0.75 | 15 | empty |
| 4 | 85 | 0.30 | 0.72 | 20 | empty |
| 5 | 66 | 0.28 | 0.73 | 15 | 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 Q4R856
- Elsewhere: UniProt Q4R856 · AlphaFold DB Q4R856
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