Q15796: Mothers against decapentaplegic homolog 2 (SMAD2)

Mothers against decapentaplegic homolog 2 (SMAD2) is a 467-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15796.

Gene
SMAD2
Organism
Homo sapiens
Length
467 residues
Mean pLDDT
77.6
Model
AF-Q15796-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.6 (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 accurate54%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions25%

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 SMAD2/SMAD4 complex, activates transcription. Promotes TGFB1-mediated transcription of odontoblastic differentiation genes in dental papilla cells (By similarity). Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. May act as a tumor suppressor in colorectal carcinoma (PubMed:8752209)

Subunit structure

Monomer; in the absence of TGF-beta (PubMed:9670020). Heterodimer; in the presence of TGF-beta (PubMed:9670020). Forms a heterodimer with co-SMAD, SMAD4, in the nucleus to form the transactivation complex SMAD2/SMAD4 (PubMed:15350224, PubMed:24324267, PubMed:9670020). Found in a complex with SMAD3 and TRIM33 upon addition of TGF-beta (PubMed:16751102). Identified in a complex that contains at…

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
6YIAX-ray1.3 ÅP=459-467
6M64X-ray1.45 ÅA/C/E=262-464
1KHXX-ray1.8 ÅA=241-467
5XODX-ray1.85 ÅA=262-458
6ZVQX-ray2.03 ÅA=241-467
1DEVX-ray2.2 ÅA/C=261-456
1U7VX-ray2.7 ÅA/C=270-467
5ZOJX-ray2.79 ÅA/B/C=262-458
7CO1X-ray3.3 ÅA/C/E=262-467
2LB3NMRB=217-224

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