Q96L21: Ribosomal protein uL16-like (RPL10L)

Ribosomal protein uL16-like (RPL10L) is a 214-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96L21.

Gene
RPL10L
Organism
Homo sapiens
Length
214 residues
Mean pLDDT
94.8
Model
AF-Q96L21-F1 v6
Model created
1 Aug 2025
PDB structures
93

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Model confidence (pLDDT)

The mean pLDDT of this model is 94.8 (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 accurate88%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Testis-specific component of the ribosome, which is required for the transition from prophase to metaphase in male meiosis I (By similarity). Compensates for the inactivated X-linked RPL10 paralog during spermatogenesis (PubMed:12490704). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:25901680, PubMed:32669547). The male germ cell-specific ribosome displays a ribosomal polypeptide exit tunnel of distinct size and charge states compared with the classical ribosome (By similarity). It is responsible for regulating the biosynthesis and folding of a subset of male germ-cell-specific proteins that are essential…

Subunit structure

Component of a male germ cell-specific 60S large ribosomal subunit (LSU), which contains RPL10L and RPL39L, instead of RPL10 and RPL39 paralogs (PubMed:23636399, PubMed:25901680, PubMed:32669547). The composition of the rest of the complex is similar to classical ribosomes (By similarity)

Subcellular location

Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8QYXEM1.78 ÅD1=1-214
8QOIEM1.9 ÅLI=1-214
9I2DEM2.19 ÅLI=1-214
9PBEEM2.19 ÅLI=2-214
7OW7EM2.2 Åp=1-214
9GULEM2.2 ÅLI=1-214
8JDKEM2.26 ÅO=1-214
9S3DEM2.32 ÅLI=1-214
9RPVEM2.35 ÅLI=1-214
9S3BEM2.38 ÅLI=1-214
8XSXEM2.4 ÅLI=1-214
8JDLEM2.42 ÅO=1-214
9S3CEM2.42 ÅLI=1-214
9QLOEM2.47 ÅLI=1-214
9P8BEM2.48 ÅLI=2-214
8JDJEM2.5 ÅO=1-214
8IFEEM2.57 Å2D=1-214
9P7DEM2.57 ÅLI=2-214
9QLQEM2.57 ÅLI=1-214
8IFDEM2.59 Å2D=1-214

Showing 20 of 93 experimental structures (best resolution first).

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