P35869: Aryl hydrocarbon receptor (AHR)

Aryl hydrocarbon receptor (AHR) is a 848-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P35869.

Gene
AHR
Organism
Homo sapiens
Length
848 residues
Mean pLDDT
56.5
Model
AF-P35869-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 56.5 (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 accurate22%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions55%

What pLDDT means and how to read it

Function

Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer (PubMed:23275542, PubMed:30373764, PubMed:32818467, PubMed:7961644). Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE) (PubMed:23275542, PubMed:30373764, PubMed:7961644). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (PubMed:12213388).…

Subunit structure

Homodimer (By similarity). Heterodimer; efficient DNA binding requires dimerization with another bHLH-PAS protein (PubMed:10395741, PubMed:28602820). Interacts with ARNT;The heterodimer ARNT:AHR binds to the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820, PubMed:34521881). Binds MYBBP1A (By similarity). Interacts with coactivators…

Subcellular location

Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8QMOEM2.76 ÅD=2-437
7ZUBEM2.85 ÅD=1-437
5NJ8X-ray3.3 ÅA/C=23-273

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