P84022: Mothers against decapentaplegic homolog 3 (SMAD3)

Mothers against decapentaplegic homolog 3 (SMAD3) is a 425-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P84022.

Gene
SMAD3
Organism
Homo sapiens
Length
425 residues
Mean pLDDT
83.6
Model
AF-P84022-F1 v6
Model created
1 Aug 2025
PDB structures
12

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.6 (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 accurate66%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions17%

What pLDDT means and how to read it

Function

Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be…

Subunit structure

Monomer; in the absence of TGF-beta (PubMed:9670020). Homooligomer; in the presence of TGF-beta (PubMed:9670020). Heterotrimer; forms a heterotrimer in the presence of TGF-beta consisting of two molecules of C-terminally phosphorylated SMAD2 or SMAD3 and one of SMAD4 to form the transcriptionally active SMAD2/SMAD3-SMAD4 complex (PubMed:11224571, PubMed:15350224, PubMed:15799969,…

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
6YIBX-ray1.7 ÅP=417-425
1MJSX-ray1.91 ÅA=229-425
5OD6X-ray2.0 ÅA/B=11-135
5ODGX-ray2.12 ÅA/B=11-135
6ZMNX-ray2.33 ÅA/B=10-136
1OZJX-ray2.4 ÅA/B=1-144
5XOCX-ray2.4 ÅA=220-416
1U7FX-ray2.6 ÅA/C=228-425
1MK2X-ray2.74 ÅA=220-425
1MHDX-ray2.8 ÅA/B=1-132
2LAJNMRB=202-211
2LB2NMRB=178-189

More AlphaFold highlights

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