Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease P protein component (Q1IY22)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease P protein component (Q1IY22) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1IY22
- Type
- protein
- Length
- 143 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Ribonuclease P protein component
- UniProt
- Q1IY22
- Pockets
- 1 · best druggability 0.39
Structure
1 distinct chain · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease P protein component | protein | 143 | 38% helix, 15% strand | Q1IY22 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.39 | 0.77 | 19 | 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 Q1IY22
- Elsewhere: UniProt Q1IY22 · AlphaFold DB Q1IY22
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