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AlphaFold monomer V2.0 prediction for 50S ribosomal protein L20, chloroplastic (Q2VEF5)
Analyse AlphaFold monomer V2.0 prediction for 50S ribosomal protein L20, chloroplastic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2VEF5
- Type
- protein
- Length
- 128 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- 50S ribosomal protein L20, chloroplastic
- UniProt
- Q2VEF5
Structure
1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 50S ribosomal protein L20, chloroplastic | protein | 128 | 77% helix, 0% strand | Q2VEF5 |
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 Q2VEF5
- Elsewhere: UniProt Q2VEF5 · AlphaFold DB Q2VEF5
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