MolNFT v1 · #406394 · protein
AlphaFold monomer V2.0 prediction for 30S ribosomal protein S4 (O52759)
O52759: “AlphaFold monomer V2.0 prediction for 30S ribosomal protein S4 (O52759)”. 2 pockets (best druggability 0.58). MolNFT v1 #406394 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- O52759
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA892Db9804620DD0b1F2F25971B016B88EDb8e33
- Molecule
- 30S ribosomal protein S4
- UniProt
- O52759
- Pockets
- 2 · best druggability 0.58
Structure
1 distinct chain · 46% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 30S ribosomal protein S4 | protein | 206 | 46% helix, 9% strand | O52759 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.58 | 0.85 | 23 | empty |
| 2 | 139 | 0.54 | 0.81 | 26 | empty |
Compared structures
- 7UNV · Pseudomonas aeruginosa 70S ribosome initiation complex bound to IF2-GDPCP (structure II-A) · an experimental structure of the same protein · chain A against d, TM-score 0.98
- 7UNW · Pseudomonas aeruginosa 70S ribosome initiation complex bound to IF2-GDPCP (structure II-B) · an experimental structure of the same protein · chain A against d, TM-score 0.98
- 7UNU · Pseudomonas aeruginosa 70S ribosome initiation complex bound to compact IF2-GDP… · an experimental structure of the same protein · chain A against d, TM-score 0.98
- 8CD1 · 70S-PHIKZ014 · an experimental structure of the same protein · chain A against d, TM-score 0.97
- 7UNR · Pseudomonas aeruginosa 70S ribosome initiation complex bound to compact IF2-GDP… · an experimental structure of the same protein · chain A against d, TM-score 0.96
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 O52759
- Elsewhere: UniProt O52759 · AlphaFold DB O52759
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