Research workbench
AlphaFold monomer V2.0 prediction for large ribosomal RNA subunit accumulation protein yced homolog 1, chloroplastic (Q9LT27)
Analyse AlphaFold monomer V2.0 prediction for large ribosomal RNA subunit accumulation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9LT27
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1Eec5F29CD795323506a0E09aeC21c942c4b00a7
- Molecule
- Large ribosomal RNA subunit accumulation protein yced homolog 1, chloroplastic
- UniProt
- Q9LT27
- Pockets
- 2 · best druggability 0.59
Structure
1 distinct chain · 12% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Large ribosomal RNA subunit accumulation protein yced homolog 1, chloroplastic | protein | 321 | 12% helix, 18% strand | Q9LT27 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 357 | 0.59 | 0.76 | 28 | empty |
| 2 | 52 | 0.25 | 0.73 | 13 | 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 Q9LT27
- Elsewhere: UniProt Q9LT27 · AlphaFold DB Q9LT27
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