P15923: Transcription factor E2-alpha (TCF3)

Transcription factor E2-alpha (TCF3) is a 654-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15923.

Gene
TCF3
Organism
Homo sapiens
Length
654 residues
Mean pLDDT
51.1
Model
AF-P15923-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 51.1 (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 accurate11%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions70%

What pLDDT means and how to read it

Function

Transcriptional regulator involved in the initiation of neuronal differentiation and mesenchymal to epithelial transition (By similarity). Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation (By similarity). Together with TCF15, required for the mesenchymal to epithelial transition (By similarity). Dimers bind DNA on E-box motifs: 5'-CANNTG-3' (By similarity). Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer (PubMed:2493990). Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription…

Subunit structure

Homodimer (PubMed:14752053, PubMed:2112746). Heterodimer; efficient DNA binding requires dimerization with another bHLH protein (By similarity). Forms a heterodimer with ASH1, TWIST1 and TWIST2 (By similarity). Forms a heterodimer with MYOG; heterodimerization enhances MYOG DNA-binding and transcriptional activities (By similarity). Forms a heterodimer with NEUROD1; the heterodimer is inhibited…

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3U5VX-ray1.7 ÅA=563-613
6MGNX-ray1.9 ÅA=561-612
2YPAX-ray2.8 ÅB=538-616
2YPBX-ray2.87 ÅB=538-616
2MH0NMRA=1-37

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