Major histocompatibility complex class I-related protein 1 (MR1) is a 341-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q95460.
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The mean pLDDT of this model is 87.5 (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 | 70% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
Antigen-presenting molecule specialized in displaying microbial pyrimidine-based metabolites to alpha-beta T cell receptors (TCR) on innate-type mucosal-associated invariant T (MAIT) cells (PubMed:19416870, PubMed:23457030, PubMed:22692454, PubMed:23051753, PubMed:24101382, PubMed:23846752, PubMed:26795251). In complex with B2M preferentially presents riboflavin-derived metabolites to semi-invariant TRAV1.2 TCRs on MAIT cells, guiding immune surveillance of the microbial metabolome at mucosal epithelial barriers (PubMed:20581831, PubMed:24101382, PubMed:24695216, PubMed:26795251). Signature pyrimidine-based microbial antigens are generated via non-enzymatic condensation of metabolite…
Heterotrimer that consists of MR1, B2M and a metabolite antigen (PubMed:23051753, PubMed:23846752, PubMed:24695216, PubMed:27043408). Major classes of metabolite ligands presented by MR1 include riboflavin-related antigens, pyrimidines and ribityl lumazines, nucleobase adducts and folate derivatives. Forms reversible covalent Schiff base complexes with microbial pyrimidine-based metabolite,…
Cell membrane, Endoplasmic reticulum membrane, Golgi apparatus membrane, Early endosome membrane, Late endosome membrane, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6PUD | X-ray | 1.8 Å | A/C=23-292 |
| 6PUG | X-ray | 1.8 Å | A/C=23-292 |
| 6PUL | X-ray | 1.84 Å | A/C=23-292 |
| 7ZT7 | X-ray | 1.84 Å | A=23-292 |
| 6PUC | X-ray | 1.85 Å | A/C=23-292 |
| 6PUH | X-ray | 1.88 Å | A/C=23-292 |
| 6W9U | X-ray | 1.89 Å | A/C=23-292 |
| 4L4V | X-ray | 1.9 Å | A/C=23-292 |
| 5U6Q | X-ray | 1.9 Å | A/C=23-292 |
| 6PUE | X-ray | 1.9 Å | A/C=23-292 |
| 6PUF | X-ray | 1.92 Å | A/C=23-292 |
| 6PUJ | X-ray | 1.92 Å | A/C=23-292 |
| 4PJE | X-ray | 1.95 Å | A/C=23-292 |
| 6W9V | X-ray | 1.95 Å | A/C=23-292 |
| 9O05 | X-ray | 1.95 Å | A/C=23-292 |
| 6PUI | X-ray | 1.96 Å | A/C=23-292 |
| 6PUM | X-ray | 1.96 Å | A/C=23-292 |
| 6PVC | X-ray | 1.96 Å | A/C=23-292 |
| 5D7J | X-ray | 1.97 Å | C/E=23-292 |
| 9O07 | X-ray | 1.97 Å | A/C=23-292 |
Showing 20 of 79 experimental structures (best resolution first).
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