P60723: Large ribosomal subunit protein uL4 (rplD)

Large ribosomal subunit protein uL4 (rplD) is a 201-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P60723.

Gene
rplD
Organism
Escherichia coli (strain K12)
Length
201 residues
Mean pLDDT
94.3
Model
AF-P60723-F1 v6
Model created
1 Aug 2025
PDB structures
626

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Model confidence (pLDDT)

The mean pLDDT of this model is 94.3 (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 accurate93%
70 to 90Confident: backbone generally right7%
50 to 70Low: treat with caution0%
Below 50Very low: often disordered regions0%

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 (PubMed:3298242). It is important during the early stages of 50S assembly (PubMed:3298242). It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (PubMed:6170935, PubMed:7556101)

Subunit structure

Part of the 50S ribosomal subunit (PubMed:10094780, PubMed:11511371, PubMed:12809609, PubMed:16272117, PubMed:24844575, PubMed:25310980, PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:3298242, PubMed:34403461, PubMed:34504068, PubMed:7556101, Ref.1). In TnaC-stalled ribosomes forms part of the binding pocket for L-Trp with the leader peptide and uL22 (PubMed:34403461, PubMed:34504068)

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8B0XEM1.55 Åe=1-201
9Q87EM1.55 Åe=1-201
8CGKEM1.64 Åe=1-201
8CGVEM1.66 Åe=1-201
8CEUEM1.83 Åe=1-201
8FTOEM1.85 Åe=1-201
8CAMEM1.86 Åe=1-201
9GHEEM1.87 Åe=1-201
8E30EM1.91 ÅM=1-201
9D89EM1.95 ÅH=1-201
8AYEEM1.96 Åe=1-201
7K00EM1.98 Åe=1-201
8CGDEM1.98 Åe=1-201
8E3OEM1.99 ÅM=1-201
8QOAEM2.0 Åe=1-201
8G6WEM2.02 Åe=1-201
8BILEM2.04 ÅC=1-201
8BIMEM2.04 ÅC=1-201
8E49EM2.05 ÅM=1-201
8E43EM2.09 ÅM=1-201

Showing 20 of 626 experimental structures (best resolution first).

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