MolNFT v1 · #364041 · protein
AlphaFold monomer V2.0 prediction for 50S ribosomal protein L2 (P94270)
P94270: “AlphaFold monomer V2.0 prediction for 50S ribosomal protein L2 (P94270)”. 2 pockets (best druggability 0.52). MolNFT v1 #364041 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P94270
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- 50S ribosomal protein L2
- UniProt
- P94270
- Pockets
- 2 · best druggability 0.52
Structure
1 distinct chain · 10% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 50S ribosomal protein L2 | protein | 277 | 10% helix, 28% strand | P94270 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 261 | 0.52 | 0.75 | 35 | empty |
| 2 | 72 | 0.41 | 0.80 | 13 | empty |
Compared structures
- 8FMW · The structure of a hibernating ribosome in the Lyme disease pathogen · an experimental structure of the same protein · chain A against AD, TM-score 0.99
- 8FN2 · The structure of a 50S ribosomal subunit in the Lyme disease pathogen Borreliella… · an experimental structure of the same protein · chain A against D, TM-score 0.99
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 P94270
- Elsewhere: UniProt P94270 · AlphaFold DB P94270
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.