G1TSG1: Large ribosomal subunit protein eL22 (RPL22)

Large ribosomal subunit protein eL22 (RPL22) is a 128-residue protein from Oryctolagus cuniculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: G1TSG1.

Gene
RPL22
Organism
Oryctolagus cuniculus
Length
128 residues
Mean pLDDT
85.4
Model
AF-G1TSG1-F1 v6
Model created
1 Aug 2025
PDB structures
50

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 85.4 (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 accurate72%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell

Subunit structure

Component of the large ribosomal subunit

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8SCBEM2.5 ÅU=1-128
9MR4EM2.65 ÅU=1-128
9RHUEM2.65 ÅQ2=1-128
8RJBEM2.69 ÅU=1-128
8VVQEM2.7 ÅT=1-128
8B6CEM2.79 ÅU=17-115
7OBREM2.8 ÅU=17-115
9BDLEM2.8 ÅAL22=17-115
9QQAEM2.8 ÅBU=1-128
8B5LEM2.86 ÅU=17-115
9Q7QEM2.86 ÅU=17-115
8P2KEM2.9 ÅBU=1-128
8RJCEM2.9 ÅU=1-128
8VVPEM2.9 ÅT=1-128
8VVTEM2.9 ÅT=1-128
9YPWEM2.9 ÅU=1-128
9YPZEM2.9 ÅU=1-128
9YQ0EM2.9 ÅU=1-128
9YQ1EM2.9 ÅU=1-128
9YPGEM3.0 ÅU=1-128

Showing 20 of 50 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.