P0A7K2: Large ribosomal subunit protein bL12 (rplL)

Large ribosomal subunit protein bL12 (rplL) is a 121-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0A7K2.

Gene
rplL
Organism
Escherichia coli (strain K12)
Length
121 residues
Mean pLDDT
77.0
Model
AF-P0A7K2-F1 v6
Model created
1 Aug 2025
PDB structures
58

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.0 (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 accurate17%
70 to 90Confident: backbone generally right60%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

The binding site for several of the GTPase factors involved in protein synthesis (IF-2, EF-Tu, EF-G and RF3). Is thus essential for accurate translation. Deletion of 1 of the L12 dimers from the ribosome (by deleting the binding site on L10) leads to decreased IF-2 association with the 70S ribosome and decreased stimulation of the GTPase activity of EF-G

Subunit structure

Homodimer. Part of the 50S ribosomal subunit; present in 4 copies per ribosome. L7/L12 forms dimers with an elongated shape. Two dimers associate with a copy of L10 to form part of the ribosomal stalk (called L8). The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Forms a pentameric L10(L12)2(L12)2 complex, where L10 forms an elongated spine to which 2 L12 dimers…

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1CTFX-ray1.7 ÅA=48-121
7N2CEM2.72 ÅLG=1-121
4V9OX-ray2.9 ÅA6=1-121
6X7KEM3.1 ÅZ=1-121
8URYEM3.1 ÅZ=1-121
4V85X-ray3.2 ÅBJ/BK/BL/BM=1-121
6I0YEM3.2 Å6=1-121
6X6TEM3.2 ÅZ=1-121
8UQLEM3.2 ÅZ=1-121
8UR0EM3.4 ÅZ=1-121
8VOOEM3.4 ÅZ=1-121
6X7FEM3.5 ÅZ=1-121
8VKVEM3.6 ÅZ=1-121
8VOREM3.6 ÅZ=1-121
8PHJEM3.67 ÅW=2-121
4V89X-ray3.7 ÅBJ/BK/BL/BM=1-121
6VU3EM3.7 ÅZ=2-31
6VYQEM3.7 ÅZ=1-121
6VYSEM3.7 ÅZ=1-121
6XDQEM3.7 ÅZ=1-121

Showing 20 of 58 experimental structures (best resolution first).

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