Research workbench
AlphaFold monomer V2.0 prediction for DNA repair and recombination protein rada (C3NFU5)
Analyse AlphaFold monomer V2.0 prediction for DNA repair and recombination protein rada… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3NFU5
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe43D264c0E4229A2c42bC24F7Fed41a1fCf1938d
- Molecule
- DNA repair and recombination protein rada
- UniProt
- C3NFU5
- Pockets
- 4 · best druggability 0.46
Structure
1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair and recombination protein rada | protein | 324 | 42% helix, 21% strand | C3NFU5 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.46 | 0.74 | 24 | empty |
| 2 | 94 | 0.41 | 0.78 | 20 | empty |
| 3 | 130 | 0.40 | 0.74 | 22 | empty |
| 4 | 76 | 0.36 | 0.77 | 19 | 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 C3NFU5
- Elsewhere: UniProt C3NFU5 · AlphaFold DB C3NFU5
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