P70662: LIM domain-binding protein 1 (Ldb1)

LIM domain-binding protein 1 (Ldb1) is a 411-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P70662.

Gene
Ldb1
Organism
Mus musculus
Length
411 residues
Mean pLDDT
71.0
Model
AF-P70662-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 71.0 (confident 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 accurate44%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions37%

What pLDDT means and how to read it

Function

Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors (PubMed:8918878, PubMed:9192866). May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions (PubMed:16815859, PubMed:18539116, PubMed:8918878, PubMed:9192866, PubMed:9315627). Plays a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1 (PubMed:12150931, PubMed:18539116, PubMed:8876198). Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression (PubMed:8918878). Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state…

Subunit structure

Interacts with ESR1 (By similarity). Forms homodimers and heterodimers (PubMed:9315627, PubMed:9468533). Interacts with and activates LHX1/LIM1 (PubMed:8918878, PubMed:9468533). Interacts with the LIM domains of ISL1 and LMO2 (PubMed:12150931, PubMed:12727888). Can assemble in a complex with LMO2 and TAL1/SCL but does not interact with TAL1/SCL directly (PubMed:9391090). Strongly interacts with…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1RUTX-ray1.3 ÅX=336-375
6PTLX-ray2.5 ÅA=50-236
4JCJX-ray3.0 ÅA/B/C=336-366
1J2ONMRA=336-375
1M3VNMRA=336-375
2JTNNMRA=331-375
2L6YNMRB=336-348
2L6ZNMRC=336-348
2LXDNMRA=336-375

More AlphaFold highlights

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