P62664: Small ribosomal subunit protein uS4 (rpsD)

Small ribosomal subunit protein uS4 (rpsD) is a 209-residue protein from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62664.

Gene
rpsD
Organism
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
Length
209 residues
Mean pLDDT
92.1
Model
AF-P62664-F1 v6
Model created
1 Aug 2025
PDB structures
22

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.1 (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 accurate78%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the body and platform of the 30S subunit

Subunit structure

Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity (By similarity)

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4V67X-ray3.0 ÅAD/CD=1-209
5J4DX-ray3.1 ÅMA/RC=1-209
6N1DX-ray3.2 ÅAS04/BS04=2-209
4V63X-ray3.21 ÅAD/CD=1-209
5V8IX-ray3.25 Å1d/2d=1-209
4V84X-ray3.4 ÅAD/CD=2-209
4V9NX-ray3.4 ÅAD/CD=2-209
4V9QX-ray3.4 ÅBD/DD=2-209
6B4VX-ray3.4 ÅMA/QC=1-209
6BOHX-ray3.4 ÅNA/SC=1-209
4V83X-ray3.5 ÅAD/CD=2-209
4V9KX-ray3.5 ÅAD/CD=2-209
4V9LX-ray3.5 ÅAD/CD=2-209
6BOKX-ray3.55 ÅLA/OC=1-209
4V7PX-ray3.62 ÅAD/DD=2-209
4V4IX-ray3.71 Åe=1-209
4W29X-ray3.8 ÅAD/CD=2-209
4XEJX-ray3.8 ÅAS04/BS04=2-209
4V4JX-ray3.83 Åe=1-209
4V9JX-ray3.86 ÅAD/CD=2-209

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

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