Research workbench
AlphaFold monomer V2.0 prediction for 50S ribosomal protein L3 (O26110)
Analyse AlphaFold monomer V2.0 prediction for 50S ribosomal protein L3 (O26110) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O26110
- Type
- protein
- Length
- 337 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- 50S ribosomal protein L3
- UniProt
- O26110
- Pockets
- 5 · best druggability 0.36
Structure
1 distinct chain · 13% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 50S ribosomal protein L3 | protein | 337 | 13% helix, 32% strand | O26110 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.36 | 0.75 | 20 | empty |
| 2 | 101 | 0.35 | 0.73 | 18 | empty |
| 3 | 70 | 0.33 | 0.75 | 14 | empty |
| 4 | 57 | 0.29 | 0.75 | 13 | empty |
| 5 | 64 | 0.28 | 0.73 | 15 | 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 O26110
- Elsewhere: UniProt O26110 · AlphaFold DB O26110
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