O34693: Rqc2 homolog RqcH (rqcH)

Rqc2 homolog RqcH (rqcH) is a 570-residue protein from Bacillus subtilis (strain 168). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O34693.

Gene
rqcH
Organism
Bacillus subtilis (strain 168)
Length
570 residues
Mean pLDDT
91.1
Model
AF-O34693-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.1 (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 accurate72%
70 to 90Confident: backbone generally right25%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions1%

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:31155236). 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:31155236, PubMed:35264791, PubMed:38177497). The Ala tail promotes nascent chain degradation (PubMed:31155236). RqcH, RqcP and charged tRNA(Ala) are necessary and sufficient to add an Ala tail to a model stalled nascent peptide; does not add Val (PubMed:34255840).…

Subunit structure

Associates with isolated or stalled 50S ribosomal subunits (PubMed:31155236, PubMed:33259811, PubMed:33259810, PubMed:34255840). Binds to RqcP (PubMed:33259811, PubMed:33259810, PubMed:34255840). Interacts with ribosomal protein uL11 (PubMed:33259811, PubMed:33259810, PubMed:34255840). Displaced from the 50S subunit by thiostrepton (PubMed:33259810, PubMed:34255840). In crystallized 50S subunits…

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7AS8EM2.9 Å0=1-570
7AQCEM2.99 ÅR=1-570
7AQDEM3.1 ÅR=1-570
7OPEEM3.2 Å0=1-570
8S1UEM3.4 ÅH=1-570
7AS9EM3.5 Å0=1-570
7ASAEM3.5 Å0=1-570

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