Q5SHN9: Large ribosomal subunit protein uL4 (rplD)

Large ribosomal subunit protein uL4 (rplD) is a 210-residue protein from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5SHN9.

Gene
rplD
Organism
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Length
210 residues
Mean pLDDT
92.4
Model
AF-Q5SHN9-F1 v6
Model created
1 Aug 2025
PDB structures
270

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.4 (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 right10%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity)

Subunit structure

Part of the 50S ribosomal subunit

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9NO7EM2.13 ÅF=1-210
4Y4OX-ray2.3 Å1F/2F=1-210
8CVLX-ray2.3 Å1F/2F=1-210
8FC6X-ray2.35 Å1F/2F=1-210
8VTWX-ray2.35 Å1F/2F=1-210
4W2FX-ray2.4 ÅBF/DF=1-210
6XHVX-ray2.4 Å1F/2F=1-210
7RQAX-ray2.4 Å1F/2F=1-210
7RQEX-ray2.4 Å1F/2F=1-210
8CVJX-ray2.4 Å1F/2F=1-210
8VTUX-ray2.4 Å1F/2F=1-210
8VTXX-ray2.4 Å1F/2F=1-210
9MTPX-ray2.4 Å1F/2F=1-210
10PXX-ray2.45 Å1F/2F=1-210
7RQBX-ray2.45 Å1F/2F=1-210
8FC4X-ray2.45 Å1F/2F=1-210
8G2AX-ray2.45 Å1F/2F=1-210
9D0IX-ray2.45 Å1F/2F=1-210
4Y4PX-ray2.5 Å1F/2F=1-210
6XHWX-ray2.5 Å1F/2F=1-210

Showing 20 of 270 experimental structures (best resolution first).

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