Q14684: Ribosomal RNA processing protein 1 homolog B (RRP1B)

Ribosomal RNA processing protein 1 homolog B (RRP1B) is a 758-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14684.

Gene
RRP1B
Organism
Homo sapiens
Length
758 residues
Mean pLDDT
59.5
Model
AF-Q14684-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 59.5 (low 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 accurate25%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions54%

What pLDDT means and how to read it

Function

Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (PubMed:20040599). Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (PubMed:20926688). Involved in regulation of mRNA splicing (By similarity). Inhibits SIPA1 GTPase activity (By similarity). Involved in regulating expression of extracellular matrix genes (By similarity). Associates with chromatin and may play a role in modulating chromatin structure (PubMed:19710015)

Subunit structure

Interacts with the transcriptional activator E2F1 (PubMed:20040599). Interacts with serine/threonine-protein phosphatase PP1 subunits PPP1CB and PPP1CC but not with PPP1CA (PubMed:20926688). Interacts with 60S ribosomal proteins RPL5 and RPL27, ribosomal processing protein RRP1/NNP1 and other nucleolar proteins including NOP2/NOL1 and FBL (PubMed:20926688). Also interacts with nucleolar protein…

Subcellular location

Nucleus, nucleolus, Nucleus, nucleoplasm, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7T0YX-ray1.8 ÅB/D=682-727

More AlphaFold highlights

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