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AlphaFold monomer V2.0 prediction for 50S ribosomal protein L2, chloroplastic (P0C497)
Analyse AlphaFold monomer V2.0 prediction for 50S ribosomal protein L2, chloroplastic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0C497
- Type
- protein
- Length
- 273 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- 50S ribosomal protein L2, chloroplastic
- UniProt
- P0C497
- Pockets
- 4 · best druggability 0.51
Structure
1 distinct chain · 6% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 50S ribosomal protein L2, chloroplastic | protein | 273 | 6% helix, 28% strand | P0C497 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 275 | 0.51 | 0.74 | 26 | empty |
| 2 | 84 | 0.37 | 0.76 | 25 | empty |
| 3 | 106 | 0.35 | 0.74 | 18 | empty |
| 4 | 55 | 0.29 | 0.75 | 12 | 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 P0C497
- Elsewhere: UniProt P0C497 · AlphaFold DB P0C497
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