P60624: Large ribosomal subunit protein uL24 (rplX)

Large ribosomal subunit protein uL24 (rplX) is a 104-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P60624.

Gene
rplX
Organism
Escherichia coli (strain K12)
Length
104 residues
Mean pLDDT
93.6
Model
AF-P60624-F1 v6
Model created
1 Aug 2025
PDB structures
582

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Model confidence (pLDDT)

The mean pLDDT of this model is 93.6 (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 accurate90%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro

Subunit structure

Part of the 50S ribosomal subunit (PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:24844575, PubMed:25310980, PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:391595). Might contact the SecYEG translocation complex when it is docked with the ribosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8B0XEM1.55 Åt=1-104
9Q87EM1.55 Åt=1-104
8CGKEM1.64 Åt=1-104
8CGVEM1.66 Åt=1-104
8CEUEM1.83 Åt=1-104
8FTOEM1.85 Åt=1-104
8CAMEM1.86 Åt=1-104
9GHEEM1.87 Åt=1-104
9D89EM1.95 Åt=2-103
8AYEEM1.96 Åt=1-104
7K00EM1.98 Åt=1-104
8CGDEM1.98 Åt=1-104
8QOAEM2.0 Åt=1-104
8G6WEM2.02 Åt=1-104
8BILEM2.04 ÅR=1-104
8BIMEM2.04 ÅR=1-104
8G6YEM2.09 Åt=1-104
4YBBX-ray2.1 ÅCV/DV=2-103
6XZ7EM2.1 ÅU=2-103
7QQ3EM2.1 Åc=1-104

Showing 20 of 582 experimental structures (best resolution first).

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