Transferrin receptor protein 1 (TFRC) is a 760-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02786.
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The mean pLDDT of this model is 86.7 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 75% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738, PubMed:41772062). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron…
Homodimer; disulfide-linked. Binds one transferrin or HFE molecule per subunit. Binds the HLA class II histocompatibility antigen, DR1. Interacts with SH3BP3. Interacts with STEAP3; facilitates TFRC endocytosis in erythroid precursor cells (PubMed:26642240). Interacts with GRM2 (PubMed:36779763). Interacts with SNX32; the interaction is involved in intracellular trafficking of the receptor…
Cell membrane, Melanosome, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6OKD | X-ray | 1.85 Å | A/B=121-760 |
| 8P0Z | X-ray | 1.88 Å | A=197-299, A=332-377 |
| 6Y76 | X-ray | 1.98 Å | A/B=197-378 |
| 9GH7 | X-ray | 2.08 Å | A=89-760 |
| 3KAS | X-ray | 2.4 Å | A=121-760 |
| 6WRV | X-ray | 2.47 Å | A/B/E=121-759 |
| 7ZQS | EM | 2.54 Å | B/D=1-760 |
| 1DE4 | X-ray | 2.8 Å | C/F/I=121-760 |
| 6WRW | X-ray | 2.84 Å | A/B=121-760 |
| 6WRX | X-ray | 3.07 Å | A/B=121-760 |
| 1CX8 | X-ray | 3.2 Å | A/B/C/D/E/F/G/H=122-760 |
| 3S9L | X-ray | 3.22 Å | A/B=120-760 |
| 3S9N | X-ray | 3.25 Å | A/B=120-760 |
| 3S9M | X-ray | 3.32 Å | A/B=120-760 |
| 6W3H | X-ray | 3.38 Å | C/D=188-296 |
| 6D03 | EM | 3.68 Å | A/B=121-760 |
| 6D04 | EM | 3.74 Å | A/B=121-760 |
| 6D05 | EM | 3.8 Å | A/B=121-760 |
| 6H5I | EM | 3.9 Å | Ab/Aq=121-760 |
| 6GSR | EM | 5.5 Å | Ab/Aq=121-760 |
Showing 20 of 22 experimental structures (best resolution first).
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