Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease P protein component (A3MS22)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease P protein component (A3MS22) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3MS22
- Type
- protein
- Length
- 136 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4ccf07E1804Dc60f0201B86045710249a508B4e8
- Molecule
- Ribonuclease P protein component
- UniProt
- A3MS22
- Pockets
- 1 · best druggability 0.49
Structure
1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease P protein component | protein | 136 | 41% helix, 16% strand | A3MS22 |
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 | 52 | 0.49 | 0.86 | 15 | 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 A3MS22
- Elsewhere: UniProt A3MS22 · AlphaFold DB A3MS22
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