Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease P protein component 3 (B0R596)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease P protein component 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0R596
- Type
- protein
- Length
- 232 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x88fe8ff7C224116F2784290d6D1Dc3f30f7E3B0b
- Molecule
- Ribonuclease P protein component 3
- UniProt
- B0R596
- Pockets
- 1 · best druggability 0.45
Structure
1 distinct chain · 49% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease P protein component 3 | protein | 232 | 49% helix, 18% strand | B0R596 |
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 | 83 | 0.45 | 0.80 | 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 B0R596
- Elsewhere: UniProt B0R596 · AlphaFold DB B0R596
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