Q15797: Mothers against decapentaplegic homolog 1 (SMAD1)

Mothers against decapentaplegic homolog 1 (SMAD1) is a 465-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15797.

Gene
SMAD1
Organism
Homo sapiens
Length
465 residues
Mean pLDDT
81.2
Model
AF-Q15797-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.2 (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 accurate63%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

Transcriptional modulator that plays a role in various cellular processes, including embryonic development, cell differentiation, and tissue homeostasis (PubMed:9335504). Upon BMP ligand binding to their receptors at the cell surface, is phosphorylated by activated type I BMP receptors (BMPRIs) and associates with SMAD4 to form a heteromeric complex which translocates into the nucleus acting as transcription factor (PubMed:33667543). In turn, the hetero-trimeric complex recognizes cis-regulatory elements containing Smad Binding Elements (SBEs) to modulate the outcome of the signaling network (PubMed:33667543). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor…

Subunit structure

Found in a complex with SMAD4 and YY1. Interacts with HGS, NANOG and ZCCHC12 (By similarity). Upon C-terminus phosphorylation: forms trimers with another SMAD1 and the co-SMAD SMAD4 (PubMed:21454478, PubMed:33667543). Interacts with PEBP2-alpha subunit, CREB-binding protein (CBP), p300, SMURF1, SMURF2, USP15 and HOXC8. Associates with ZNF423 or ZNF521 in response to BMP2 leading to activate…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3Q4AX-ray1.54 ÅC=456-465
3Q47X-ray1.7 ÅC=456-464
1KHUX-ray2.5 ÅA/B/C/D=248-465
5ZOKX-ray2.85 ÅA/C=259-462
2LAWNMRB=222-233
2LAXNMRB=201-209
2LAYNMRB=201-209
2LAZNMRB=210-217
2LB0NMRB=208-217
2LB1NMRB=220-233

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