P26342: Transforming growth factor beta receptor type 3 (Tgfbr3)

Transforming growth factor beta receptor type 3 (Tgfbr3) is a 853-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P26342.

Gene
Tgfbr3
Organism
Rattus norvegicus
Length
853 residues
Mean pLDDT
71.6
Model
AF-P26342-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 71.6 (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 accurate27%
70 to 90Confident: backbone generally right36%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions27%

What pLDDT means and how to read it

Function

Cell surface receptor that regulates diverse cellular processes including cell proliferation, differentiation, migration, and apoptosis. Initiates BMP, inhibin, and TGF-beta signaling pathways by interacting with different ligands including TGFB1, BMP2, BMP5, BMP7 or GDF5. Alternatively, acts as a cell surface coreceptor for BMP ligands, serving to enhance ligand binding by differentially regulating BMPR1A/ALK3 and BMPR1B/ALK6 receptor trafficking. Promotes epithelial cell adhesion, focal adhesion formation and integrin signaling during epithelial cell spreading on fibronectin. By interacting with the scaffolding protein beta-arrestin2/ARRB2, regulates migration or actin cytoskeleton and…

Subunit structure

Forms homodimers and homooligomers. Interacts with DYNLT4. Interacts with integrin ITGA5:ITGB1; this interaction promotes the internalization and trafficking of ITGA5:ITGB1 into endocytic vesicles. Interacts with TGFB1, BMP2, BMP5, BMP7 or GDF5 and inhibin A via the ligand binding domains. Interacts with ALK3/BMPR1A; this interaction results in the cell surface retention of BMPR1A. Interacts…

Subcellular location

Cell membrane, Secreted, Secreted, extracellular space, extracellular matrix

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8DC0X-ray1.93 ÅA=590-757
3QW9X-ray2.0 ÅA/B=591-763
9FDYEM3.4 ÅC=31-360

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