Q5SHZ1: Large ribosomal subunit protein bL25 (rplY)

Large ribosomal subunit protein bL25 (rplY) is a 206-residue protein from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5SHZ1.

Gene
rplY
Organism
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Length
206 residues
Mean pLDDT
85.8
Model
AF-Q5SHZ1-F1 v6
Model created
1 Aug 2025
PDB structures
268

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.8 (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 accurate69%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

This is one of 3 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit

Subunit structure

Part of the 50S ribosomal subunit. Contacts the 5S rRNA; has been isolated in a complex with 5S rRNA and uL5, 5S rRNA and DNA binding protein II; 5S rRNA and uL18; 5S rRNA, uL5 and DNA binding protein II (Ref.4)

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9NO7EM2.13 ÅZ=1-206
4Y4OX-ray2.3 Å1Z/2Z=1-206
8CVLX-ray2.3 Å1Z/2Z=1-206
8FC6X-ray2.35 Å1Z/2Z=1-206
8VTWX-ray2.35 Å1Z/2Z=1-206
4W2FX-ray2.4 ÅBZ/DZ=1-206
6XHVX-ray2.4 Å1Z/2Z=1-206
7RQAX-ray2.4 Å1Z/2Z=1-206
7RQEX-ray2.4 Å1Z/2Z=1-206
8CVJX-ray2.4 Å1Z/2Z=1-206
8VTUX-ray2.4 Å1Z/2Z=1-206
8VTXX-ray2.4 Å1Z/2Z=1-206
9MTPX-ray2.4 Å1Z/2Z=1-206
10PXX-ray2.45 Å1Z/2Z=1-206
7RQBX-ray2.45 Å1Z/2Z=1-206
8FC4X-ray2.45 Å1Z/2Z=1-206
8G2AX-ray2.45 Å1Z/2Z=1-206
9D0IX-ray2.45 Å1Z/2Z=1-206
4Y4PX-ray2.5 Å1Z/2Z=1-206
6XHWX-ray2.5 Å1Z/2Z=1-206

Showing 20 of 268 experimental structures (best resolution first).

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