P37557: RQC P-site tRNA stabilizing factor (rqcP)

RQC P-site tRNA stabilizing factor (rqcP) is a 86-residue protein from Bacillus subtilis (strain 168). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P37557.

Gene
rqcP
Organism
Bacillus subtilis (strain 168)
Length
86 residues
Mean pLDDT
90.8
Model
AF-P37557-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 90.8 (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 accurate76%
70 to 90Confident: backbone generally right23%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Key component of the ribosome quality control system (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes and their subsequent degradation (PubMed:33259811, PubMed:33259810, PubMed:34255840). RqcH recruits Ala-charged tRNA, and with RqcP directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal alanine extensions (Ala tail) (PubMed:33259811, PubMed:33259810, PubMed:34255840). The Ala tail promotes nascent chain degradation (PubMed:34255840). RqcP is associated with the translocation-like movement of the peptidyl-tRNA from the A-site into the P-site…

Subunit structure

Associates with stalled 50S ribosomal subunits (PubMed:33259811, PubMed:33259810, PubMed:34255840). Binds to RqcH, 23S rRNA and the P-site tRNA (PubMed:33259811, PubMed:33259810, PubMed:34255840). Does not require RqcH for association with 50S subunits (PubMed:34255840). Crystallized 50S subunits are variously associated with an A/P-site tRNA with or without RqcH, as well as with P- and E-site…

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7AS8EM2.9 Å1=1-86
7AQCEM2.99 ÅY=1-86
7OPEEM3.2 Å1=1-86
7ASAEM3.5 Å1=1-86

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