P27782: Lymphoid enhancer-binding factor 1 (Lef1)

Lymphoid enhancer-binding factor 1 (Lef1) is a 397-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P27782.

Gene
Lef1
Organism
Mus musculus
Length
397 residues
Mean pLDDT
57.2
Model
AF-P27782-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 57.2 (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 accurate16%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution29%
Below 50Very low: often disordered regions52%

What pLDDT means and how to read it

Function

Transcription factor that binds DNA in a sequence-specific manner (By similarity). Participates in the Wnt signaling pathway (PubMed:11445543). Activates transcription of target genes in the presence of CTNNB1 and EP300 (PubMed:12446687). PIASG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1 (PubMed:11731474). TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1 (By similarity). Regulates T-cell receptor alpha enhancer function (By similarity). Required for IL17A expressing gamma-delta T-cell maturation and development, via binding to regulator loci of BLK to modulate expression (PubMed:23562159). Acts as a positive regulator of odontoblast…

Subunit structure

Binds the armadillo repeat of CTNNB1 and forms a stable complex. Binds TLE1, ALYREF/THOC4, MDFI and MDFIC (By similarity). Interacts with NLK (By similarity). Interacts with EP300 and PIASG. Interacts with DAZAP2 (PubMed:19304756)

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3OUXX-ray2.4 ÅB=1-63
3OUWX-ray2.91 ÅB=1-63
2LEFNMRA=295-380

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