Research workbench
AlphaFold monomer V2.0 prediction for multiple RNA-binding domain- containing protein 1 (P0CR17)
Analyse AlphaFold monomer V2.0 prediction for multiple RNA-binding domain- containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CR17
- Type
- protein
- Length
- 769 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6A9Ec001Bc00FA7B5ca9B36332E57e2641f2d127
- Molecule
- Multiple RNA-binding domain-containing protein 1
- UniProt
- P0CR17
- Pockets
- 7 · best druggability 0.59
Structure
1 distinct chain · 30% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multiple RNA-binding domain-containing protein 1 | protein | 769 | 30% helix, 18% strand | P0CR17 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.59 | 0.79 | 28 | empty |
| 2 | 148 | 0.48 | 0.77 | 23 | empty |
| 3 | 179 | 0.46 | 0.75 | 25 | empty |
| 4 | 73 | 0.38 | 0.78 | 17 | empty |
| 5 | 70 | 0.33 | 0.75 | 14 | 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 P0CR17
- Elsewhere: UniProt P0CR17 · AlphaFold DB P0CR17
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