P21465: Small ribosomal subunit protein uS3 (rpsC)

Small ribosomal subunit protein uS3 (rpsC) is a 218-residue protein from Bacillus subtilis (strain 168). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P21465.

Gene
rpsC
Organism
Bacillus subtilis (strain 168)
Length
218 residues
Mean pLDDT
90.5
Model
AF-P21465-F1 v6
Model created
1 Aug 2025
PDB structures
22

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 90.5 (very high overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate82%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions4%

What pLDDT means and how to read it

Function

Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation

Subunit structure

Part of the 30S ribosomal subunit (PubMed:30126986). Forms a tight complex with proteins S10 and S14 (By similarity)

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
8QCQEM2.3 Åc=1-206
9FY1EM2.3 Åc=1-218
9FY2EM2.3 Åc=1-218
9FY3EM2.8 Åc=1-218
8BUUEM2.9 Åc=1-218
6HA1EM3.1 Åc=1-218
8CDUEM3.1 ÅE=1-218
7O5BEM3.33 ÅC=1-218
8QPPEM3.4 ÅC=1-218
6HA8EM3.5 Åc=1-218
7QV1EM3.5 Åc=1-218
7QV2EM3.5 Åc=1-218
8CECEM3.57 ÅH=1-218
8R55EM3.57 ÅC=1-218
8CEEEM3.7 ÅE=1-218
5NJTEM3.8 ÅC=2-211
3J9WEM3.9 ÅAC=1-218
8CEDEM4.15 ÅE=1-218
6HTQEM4.5 Åc=2-207
7QGUEM4.75 Åh=1-218

Showing 20 of 22 experimental structures (best resolution first).

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.