P46781: Small ribosomal subunit protein uS4 (RPS9)

Small ribosomal subunit protein uS4 (RPS9) is a 194-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P46781.

Gene
RPS9
Organism
Homo sapiens
Length
194 residues
Mean pLDDT
88.1
Model
AF-P46781-F1 v6
Model created
1 Aug 2025
PDB structures
188

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.1 (confident 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 accurate74%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)

Subunit structure

Component of the small ribosomal subunit (PubMed:23636399). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797)

Subcellular location

Cytoplasm, Nucleus, nucleolus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8GLPEM1.67 ÅSJ=1-194
8QOIEM1.9 ÅSJ=1-194
9O3WEM1.9 ÅSJ=1-194
8YOOEM2.0 ÅSJ=1-194
9C3HEM2.0 ÅSJ=1-194
7R4XEM2.15 ÅJ=1-194
9I2DEM2.19 ÅSJ=1-194
9PBEEM2.19 ÅSJ=2-186
8YOPEM2.2 ÅSJ=1-194
9O3YEM2.2 ÅSJ=1-194
8JDKEM2.26 Å6=1-194
8G5YEM2.29 ÅSJ=1-194
9S3DEM2.32 ÅSJ=1-194
9RPVEM2.35 ÅRJ/SJ=1-194
9S3BEM2.38 ÅSJ=1-194
8K2CEM2.4 ÅSJ=1-194
8XSXEM2.4 ÅSJ=1-194
9SPFEM2.4 ÅSJ=1-194
9SPIEM2.4 ÅSJ=1-194
8JDLEM2.42 Å6=1-194

Showing 20 of 188 experimental structures (best resolution first).

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