P50481: LIM/homeobox protein Lhx3 (Lhx3)

LIM/homeobox protein Lhx3 (Lhx3) is a 400-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P50481.

Gene
Lhx3
Organism
Mus musculus
Length
400 residues
Mean pLDDT
68.3
Model
AF-P50481-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.3 (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 accurate33%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions37%

What pLDDT means and how to read it

Function

Transcription factor (PubMed:10593900, PubMed:12150931, PubMed:18539116). Recognizes and binds to the consensus sequence motif 5'-AATTAATTA-3' in the regulatory elements of target genes, such as glycoprotein hormones alpha chain CGA and visual system homeobox CHX10, positively modulating transcription; transcription can be co-activated by LDB2 (PubMed:10593900, PubMed:18539116, PubMed:9192866). Synergistically enhances transcription from the prolactin promoter in cooperation with POU1F1/Pit-1 (PubMed:7708713). Required for the establishment of the specialized cells of the pituitary gland and the nervous system (By similarity). Involved in the development of interneurons and motor neurons…

Subunit structure

Interacts with POU1F1 (By similarity). At neuronal promoters, interacts with LDB1, in motor neurons LDB1 is displaced by ISL1 and a ternary complex is formed in which ISL1 contacts both LHX3 and LDB1; allosteric structural changes in the DNA binding domain of LHX3, induced by the ISL1-LHX3 interaction, may explain differences in sequence specificity of the different complexes (PubMed:12150931,…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2RGTX-ray2.05 ÅA/B=28-153
2JTNNMRA=28-153

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