Cation-independent mannose-6-phosphate receptor (IGF2R) is a 2491-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P11717.
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The mean pLDDT of this model is 73.1 (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 | 3% |
| 70 to 90 | Confident: backbone generally right | 69% |
| 50 to 70 | Low: treat with caution | 18% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
Mediates the transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes (PubMed:18817523, PubMed:2963003). Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex (PubMed:18817523, PubMed:2963003). The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer (PubMed:18817523). This receptor also binds IGF2 (PubMed:18046459). Acts as a positive regulator of T-cell…
Binds HA-I and HA-II plasma membrane adapters (By similarity). Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3. Interacts with the heterotrimeric retromer cargo-selective complex (CSC), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35; which is involved in retrograde trafficking of the receptor from endosomes to the Golgi apparatus (Probable). Interacts with SNX32;…
Golgi apparatus membrane, Endosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1GP0 | X-ray | 1.4 Å | A=1508-1650 |
| 6Z30 | X-ray | 1.5 Å | A=1222-1510 |
| 1E6F | X-ray | 1.75 Å | A/B=1508-1650 |
| 1GQB | X-ray | 1.8 Å | A/B=1508-1650 |
| 1GP3 | X-ray | 1.95 Å | A=1508-1650 |
| 1JWG | X-ray | 2.0 Å | C/D=2479-2491 |
| 6N5X | X-ray | 2.05 Å | A=2347-2377 |
| 6N5Y | X-ray | 2.26 Å | A=2347-2377 |
| 1LF8 | X-ray | 2.3 Å | E/F/G/H=2480-2491 |
| 1JPL | X-ray | 2.4 Å | E/F/G/H=2480-2491 |
| 6V02 | X-ray | 2.46 Å | A=43-763 |
| 6P8I | X-ray | 2.54 Å | A=36-763 |
| 6Z31 | X-ray | 2.56 Å | A/B=1082-1220 |
| 5IEI | X-ray | 2.8 Å | A=1508-1649 |
| 2V5O | X-ray | 2.91 Å | A=1508-2128 |
| 2V5N | X-ray | 3.2 Å | A=1508-1800 |
| 6Z32 | X-ray | 3.47 Å | A/B=927-1649 |
| 2V5P | X-ray | 4.1 Å | A/B=1508-1993 |
| 8AFZ | EM | 10.0 Å | C=2347-2377 |
| 2CNJ | NMR | D=1508-1651 |
Showing 20 of 24 experimental structures (best resolution first).
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