Q16236: Nuclear factor erythroid 2-related factor 2 (NFE2L2)

Nuclear factor erythroid 2-related factor 2 (NFE2L2) is a 605-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q16236.

Gene
NFE2L2
Organism
Homo sapiens
Length
605 residues
Mean pLDDT
60.5
Model
AF-Q16236-F1 v6
Model created
1 Aug 2025
PDB structures
23

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Model confidence (pLDDT)

The mean pLDDT of this model is 60.5 (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 accurate21%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions48%

What pLDDT means and how to read it

Function

Transcription factor that plays a key role in the response to oxidative stress: binds to antioxidant response (ARE) elements present in the promoter region of many cytoprotective genes, such as phase 2 detoxifying enzymes, and promotes their expression, thereby neutralizing reactive electrophiles (PubMed:11035812, PubMed:19489739, PubMed:29018201, PubMed:31398338). In normal conditions, ubiquitinated and degraded in the cytoplasm by the BCR(KEAP1) complex (PubMed:11035812, PubMed:15601839, PubMed:29018201). In response to oxidative stress, electrophile metabolites inhibit activity of the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2, heterodimerization with one of the…

Subunit structure

Heterodimer; heterodimerizes with small Maf proteins (By similarity). Interacts (via the bZIP domain) with MAFG and MAFK; required for binding to antioxidant response elements (AREs) on DNA (By similarity). Interacts with KEAP1; the interaction is direct and promotes ubiquitination by the BCR(KEAP1) E3 ubiquitin ligase complex (PubMed:15601839, PubMed:16888629). Forms a ternary complex with…

Subcellular location

Cytoplasm, cytosol, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2FLUX-ray1.5 ÅP=69-84
9T8YX-ray1.79 ÅB=340-351
4IFLX-ray1.8 ÅP=69-84
8HZ8X-ray1.81 ÅC=172-175
7K2AX-ray1.9 ÅP=76-83
5WFVX-ray1.91 ÅP=76-84
7K2KX-ray1.98 ÅP=77-82
7K2EX-ray2.03 ÅP=77-82
8EJRX-ray2.08 ÅC=76-82
7K2CX-ray2.11 ÅP=77-82
7K28X-ray2.15 ÅP=77-84
9T95X-ray2.15 ÅB=340-351
3ZGCX-ray2.2 ÅC=76-82
7K29X-ray2.2 ÅP=76-84
7K2DX-ray2.21 ÅP=77-82
7X5EX-ray2.3 ÅB/F=452-560
7X5GX-ray2.3 ÅB/F=452-560
7K2BX-ray2.31 ÅP=77-83
6T7VX-ray2.6 ÅI=76-84
7X5FX-ray2.6 ÅB/F=452-560

Showing 20 of 23 experimental structures (best resolution first).

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