Q13485: Mothers against decapentaplegic homolog 4 (SMAD4)

Mothers against decapentaplegic homolog 4 (SMAD4) is a 552-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13485.

Gene
SMAD4
Organism
Homo sapiens
Length
552 residues
Mean pLDDT
73.4
Model
AF-Q13485-F1 v6
Model created
1 Aug 2025
PDB structures
12

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.4 (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 accurate50%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions33%

What pLDDT means and how to read it

Function

In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (By similarity). Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the…

Subunit structure

Monomer; in the absence of TGF-beta activation (PubMed:9670020). Heterotrimer; on TGF-beta activation (PubMed:15799969). Heterotrimer composed of two molecules of a C-terminally phosphorylated R-SMAD molecule, SMAD2 or SMAD3, and one molecule of SMAD4 to form the transcriptional active SMAD2/SMAD3-SMAD4 complex (PubMed:15350224, PubMed:15799969). Found in a ternary complex composed of SMAD4,…

Subcellular location

Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6YICX-ray1.6 ÅP=398-406
5MEYX-ray2.05 ÅA=10-140
1YGSX-ray2.1 ÅA=319-552
5UWUX-ray2.24 ÅD=133-149
1U7FX-ray2.6 ÅB=314-552
5C4VX-ray2.6 ÅA/C/E=314-549
1DD1X-ray2.62 ÅA/B/C=285-552
1U7VX-ray2.7 ÅB=314-549
1MR1X-ray2.85 ÅA/B=319-552
5MEZX-ray2.98 ÅA/B=10-140
1G88X-ray3.0 ÅA/B/C=285-552
5MF0X-ray3.03 ÅA/B=10-140

More AlphaFold highlights

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