Research workbench
AlphaFold monomer V2.0 prediction for ribosomal protein S12 methylthiotransferase rimo (Q12A25)
Analyse AlphaFold monomer V2.0 prediction for ribosomal protein S12… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12A25
- Type
- protein
- Length
- 469 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97adc63ca77a299Af67cde70c5307C7EBfdc0184
- Molecule
- Ribosomal protein S12 methylthiotransferase rimo
- UniProt
- Q12A25
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosomal protein S12 methylthiotransferase rimo | protein | 469 | 35% helix, 21% strand | Q12A25 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 588 | 0.77 | 0.83 | 50 | empty |
| 2 | 100 | 0.43 | 0.78 | 26 | empty |
| 3 | 73 | 0.33 | 0.75 | 21 | 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 Q12A25
- Elsewhere: UniProt Q12A25 · AlphaFold DB Q12A25
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