Advanced glycosylation end product-specific receptor (AGER) is a 404-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15109.
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The mean pLDDT of this model is 82.8 (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 | 57% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
Cell surface pattern recognition receptor that senses endogenous stress signals with a broad ligand repertoire including advanced glycation end products, S100 proteins, high-mobility group box 1 protein/HMGB1, amyloid beta/APP oligomers, nucleic acids, histones, phospholipids and glycosaminoglycans (PubMed:27572515, PubMed:28515150, PubMed:34743181, PubMed:35974093, PubMed:24081950). Advanced glycation end products (AGEs) are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes (PubMed:21565706). These ligands accumulate at inflammatory sites during the pathogenesis of various diseases including diabetes, vascular…
Constitutive homodimer; disulfide-linked (PubMed:24081950). Forms homooligomers (PubMed:24081950). Interacts with S100A1 and APP (By similarity). Interacts with S100B, S100A12 and S100A14. Interacts with TIRAP (PubMed:21829704). Interacts with HMGB1 (PubMed:34743181). Interacts with LGP2; this interaction plays an important role in AGER-mediated pro-inflammatory responses and cytokine release…
Cell membrane, Cell projection, phagocytic cup, Early endosome, Nucleus, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5D7F | X-ray | 1.3 Å | P=65-79 |
| 3O3U | X-ray | 1.5 Å | N=23-231 |
| 6XQ1 | X-ray | 1.51 Å | A/B=23-231 |
| 6XQ3 | X-ray | 1.71 Å | A/B=23-231 |
| 6XQ5 | X-ray | 1.8 Å | A/B=23-231 |
| 6XQ7 | X-ray | 1.8 Å | A/B=23-231 |
| 6XQ8 | X-ray | 1.82 Å | A/B=23-231 |
| 3CJJ | X-ray | 1.85 Å | A=23-240 |
| 6XQ6 | X-ray | 1.9 Å | A/B=23-231 |
| 7LML | X-ray | 2.15 Å | A/B=23-231 |
| 4P2Y | X-ray | 2.3 Å | A=23-323 |
| 6XQ9 | X-ray | 2.3 Å | A/B=23-231 |
| 4LP4 | X-ray | 2.4 Å | A/B=23-231 |
| 4YBH | X-ray | 2.4 Å | A=23-323 |
| 7LMW | X-ray | 2.5 Å | A/B=23-231 |
| 4XYN | X-ray | 2.55 Å | P=54-68 |
| 4OF5 | X-ray | 2.8 Å | A/B=23-237 |
| 4OFV | X-ray | 3.1 Å | A/B=23-237 |
| 4OI7 | X-ray | 3.1 Å | A/B=23-237 |
| 4OI8 | X-ray | 3.1 Å | A/B=23-237 |
Showing 20 of 32 experimental structures (best resolution first).
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