Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease P protein component (Q5N605)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease P protein component (Q5N605) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5N605
- Type
- protein
- Length
- 122 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Ribonuclease P protein component
- UniProt
- Q5N605
- Pockets
- 1 · best druggability 0.59
Structure
1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease P protein component | protein | 122 | 36% helix, 21% strand | Q5N605 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 274 | 0.59 | 0.78 | 24 | 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 Q5N605
- Elsewhere: UniProt Q5N605 · AlphaFold DB Q5N605
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