Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease P protein component 2 (Q5JJ62)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease P protein component 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5JJ62
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Ribonuclease P protein component 2
- UniProt
- Q5JJ62
Structure
1 distinct chain · 38% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease P protein component 2 | protein | 120 | 38% helix, 30% strand | Q5JJ62 |
Compared structures
- 3WZ0 · On archaeal homologs of the human RNase P proteins POP5 and RPP30 in the… · an experimental structure of the same protein · chain A against C, TM-score 0.87
- 3WZ0 · On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the… · an experimental structure of the same protein · chain A against C, TM-score 0.87
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 Q5JJ62
- Elsewhere: UniProt Q5JJ62 · AlphaFold DB Q5JJ62
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