Research workbench
AlphaFold monomer V2.0 prediction for 50S ribosomal protein L23 (Q2YYP8)
Analyse AlphaFold monomer V2.0 prediction for 50S ribosomal protein L23 (Q2YYP8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2YYP8
- Type
- protein
- Length
- 91 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8A26B6CB9a581dc8b6062B396e50E819766d0D4a
- Molecule
- 50S ribosomal protein L23
- UniProt
- Q2YYP8
Structure
1 distinct chain · 25% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 50S ribosomal protein L23 | protein | 91 | 25% helix, 42% strand | Q2YYP8 |
Compared structures
- 6HMA · Improved model derived from cryo-EM map of Staphylococcus aureus large ribosomal subunit · an experimental structure of the same protein · chain A against R, TM-score 0.92
- 6HMA · Improved model derived from cryo-EM MAP of staphylococcus aureus large ribosomal subunit · an experimental structure of the same protein · chain A against R, TM-score 0.92
- 6FXC · The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus… · an experimental structure of the same protein · chain A against AR, TM-score 0.90
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 Q2YYP8
- Elsewhere: UniProt Q2YYP8 · AlphaFold DB Q2YYP8
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