Research workbench
AlphaFold monomer V2.0 prediction for wd repeat and coiled-coil- containing protein (Q5RFV8)
Analyse AlphaFold monomer V2.0 prediction for wd repeat and coiled-coil- containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5RFV8
- Type
- protein
- Length
- 714 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x05D249E48b5e19C17E7AE90Ad57354470160c428
- Molecule
- Wd repeat and coiled-coil-containing protein
- UniProt
- Q5RFV8
- Pockets
- 4 · best druggability 0.72
Structure
1 distinct chain · 7% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wd repeat and coiled-coil-containing protein | protein | 714 | 7% helix, 33% strand | Q5RFV8 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 504 | 0.72 | 0.81 | 55 | empty |
| 2 | 285 | 0.55 | 0.76 | 36 | empty |
| 3 | 75 | 0.33 | 0.75 | 15 | empty |
| 4 | 68 | 0.28 | 0.73 | 21 | 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 Q5RFV8
- Elsewhere: UniProt Q5RFV8 · AlphaFold DB Q5RFV8
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