P10276: Retinoic acid receptor alpha (RARA)

Retinoic acid receptor alpha (RARA) is a 462-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P10276.

Gene
RARA
Organism
Homo sapiens
Length
462 residues
Mean pLDDT
78.1
Model
AF-P10276-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.1 (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 accurate59%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

Receptor for retinoic acid (PubMed:16417524, PubMed:19850744, PubMed:20215566, PubMed:21152046, PubMed:37478846). Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes (PubMed:21152046, PubMed:28167758, PubMed:37478846). The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (PubMed:19398580, PubMed:28167758). In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone…

Subunit structure

Heterodimer; with RXRA (via C-terminus); association with RXRA is enhanced by pulsatile shear stress (PubMed:10698945, PubMed:10882070, PubMed:15509776, PubMed:20215566, PubMed:21152046, PubMed:28167758). Binds DNA preferentially as a heterodimer (PubMed:10698945, PubMed:28167758). RXRA serves as enhancer to induce RARA binding to RARE (PubMed:30468856). Interacts with RXRG (PubMed:28167758).…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9GFEX-ray1.58 ÅA=181-415
1DSZX-ray1.7 ÅA=82-167
3KMRX-ray1.8 ÅA=176-421
5K13X-ray1.85 ÅA=181-426
7WQQX-ray1.9 ÅA=176-421
3KMZX-ray2.1 ÅA/B=176-421
9GFIX-ray2.1 ÅA=180-415
6XWGX-ray2.4 ÅD=82-167
7APOX-ray2.4 ÅA/B=176-421
1DKFX-ray2.5 ÅB=182-416
7AOSX-ray2.55 ÅB=176-421
3A9EX-ray2.75 ÅB=153-421
4DQMX-ray2.75 ÅA/C=182-415
7QAAX-ray2.76 ÅB=182-416

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