Research workbench
AlphaFold monomer V2.0 prediction for peptide chain release factor 1 (P0DD95)
Analyse AlphaFold monomer V2.0 prediction for peptide chain release factor 1 (P0DD95) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0DD95
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC418d21c18A4CAeb6393DF9d71eCef5b62524fc4
- Molecule
- Peptide chain release factor 1
- UniProt
- P0DD95
- Pockets
- 4 · best druggability 0.46
Structure
1 distinct chain · 53% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide chain release factor 1 | protein | 359 | 53% helix, 20% strand | P0DD95 |
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 | 174 | 0.46 | 0.76 | 22 | empty |
| 2 | 82 | 0.37 | 0.77 | 18 | empty |
| 3 | 78 | 0.35 | 0.76 | 15 | empty |
| 4 | 70 | 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 P0DD95
- Elsewhere: UniProt P0DD95 · AlphaFold DB P0DD95
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