P15880: Small ribosomal subunit protein uS5 (RPS2)

Small ribosomal subunit protein uS5 (RPS2) is a 293-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15880.

Gene
RPS2
Organism
Homo sapiens
Length
293 residues
Mean pLDDT
80.9
Model
AF-P15880-F1 v6
Model created
1 Aug 2025
PDB structures
184

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.9 (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 accurate62%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions17%

What pLDDT means and how to read it

Function

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (PubMed:23636399). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (PubMed:23636399). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in…

Subunit structure

Component of the small ribosomal subunit (PubMed:23636399). Interacts with zinc finger protein ZNF277 (via zinc-finger domains); the interaction is direct; the interaction is extra-ribosomal (PubMed:30530495). Interaction with ZNF277 competes with the binding of RPS2 to protein arginine methyltransferase PRMT3 (PubMed:30530495). Interacts with PRMT3 (PubMed:27697862). Interacts with PDCD2; the…

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 ÅSC=1-293
8QOIEM1.9 ÅSC=1-293
9O3WEM1.9 ÅSC=1-293
8YOOEM2.0 ÅSC=1-293
9C3HEM2.0 ÅSC=1-293
7R4XEM2.15 ÅC=1-293
9I2DEM2.19 ÅSC=1-293
9PBEEM2.19 ÅSC=59-280
8YOPEM2.2 ÅSC=1-293
9O3YEM2.2 ÅSC=1-293
8JDKEM2.26 Åz=1-293
8G5YEM2.29 ÅSC=1-293
9S3DEM2.32 ÅSC=1-293
9RPVEM2.35 ÅRC/SC=1-293
9S3BEM2.38 ÅSC=1-293
8K2CEM2.4 ÅSC=1-293
8XSXEM2.4 ÅSC=1-293
9SPFEM2.4 ÅSC=1-293
9SPIEM2.4 ÅSC=1-293
8JDLEM2.42 Åz=1-293

Showing 20 of 184 experimental structures (best resolution first).

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