Research workbench
AlphaFold monomer V2.0 prediction for 30S ribosomal protein S15, chloroplastic (B5LMR9)
Analyse AlphaFold monomer V2.0 prediction for 30S ribosomal protein S15, chloroplastic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5LMR9
- Type
- protein
- Length
- 91 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- 30S ribosomal protein S15, chloroplastic
- UniProt
- B5LMR9
- Pockets
- 1 · best druggability 0.56
Structure
1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 30S ribosomal protein S15, chloroplastic | protein | 91 | 71% helix, 0% strand | B5LMR9 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 252 | 0.56 | 0.77 | 26 | 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 B5LMR9
- Elsewhere: UniProt B5LMR9 · AlphaFold DB B5LMR9
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