Research workbench
AlphaFold monomer V2.0 prediction for POLY(RC)-binding protein 1 (Q5E9A3)
Analyse AlphaFold monomer V2.0 prediction for POLY(RC)-binding protein 1 (Q5E9A3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5E9A3
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- POLY(RC)-binding protein 1
- UniProt
- Q5E9A3
- Pockets
- 4 · best druggability 0.46
Structure
1 distinct chain · 34% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | POLY(RC)-binding protein 1 | protein | 356 | 34% helix, 17% strand | Q5E9A3 |
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 | 184 | 0.46 | 0.75 | 29 | empty |
| 2 | 138 | 0.44 | 0.76 | 20 | empty |
| 3 | 76 | 0.34 | 0.75 | 18 | empty |
| 4 | 80 | 0.34 | 0.75 | 16 | 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 Q5E9A3
- Elsewhere: UniProt Q5E9A3 · AlphaFold DB Q5E9A3
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