Research workbench
AlphaFold monomer V2.0 prediction for 30S ribosomal protein S3, chloroplastic (Q20F10)
Analyse AlphaFold monomer V2.0 prediction for 30S ribosomal protein S3, chloroplastic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q20F10
- Type
- protein
- Length
- 235 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc2962C0395C930d314F6bC5B4EC1De06497Bd7ff
- Molecule
- 30S ribosomal protein S3, chloroplastic
- UniProt
- Q20F10
- Pockets
- 4 · best druggability 0.40
Structure
1 distinct chain · 37% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 30S ribosomal protein S3, chloroplastic | protein | 235 | 37% helix, 29% strand | Q20F10 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.40 | 0.75 | 20 | empty |
| 2 | 117 | 0.40 | 0.75 | 26 | empty |
| 3 | 66 | 0.38 | 0.79 | 17 | empty |
| 4 | 62 | 0.28 | 0.73 | 14 | 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 Q20F10
- Elsewhere: UniProt Q20F10 · AlphaFold DB Q20F10
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