Research workbench
AlphaFold monomer V2.0 prediction for PRA1 family protein E (Q9FRR1)
Analyse AlphaFold monomer V2.0 prediction for PRA1 family protein E (Q9FRR1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9FRR1
- Type
- protein
- Length
- 209 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- PRA1 family protein E
- UniProt
- Q9FRR1
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PRA1 family protein E | protein | 209 | 64% helix, 0% strand | Q9FRR1 |
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 | 709 | 0.70 | 0.77 | 63 | empty |
| 2 | 224 | 0.61 | 0.80 | 26 | empty |
| 3 | 117 | 0.37 | 0.74 | 18 | empty |
| 4 | 71 | 0.29 | 0.73 | 13 | 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 Q9FRR1
- Elsewhere: UniProt Q9FRR1 · AlphaFold DB Q9FRR1
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