HLA class I histocompatibility antigen, alpha chain G (HLA-G) is a 338-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P17693.
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The mean pLDDT of this model is 90.4 (very high 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 | 81% |
| 70 to 90 | Confident: backbone generally right | 10% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Non-classical major histocompatibility class Ib molecule involved in immune regulatory processes at the maternal-fetal interface (PubMed:19304799, PubMed:23184984, PubMed:29262349). In complex with B2M/beta-2 microglobulin binds a limited repertoire of nonamer self-peptides derived from intracellular proteins including histones and ribosomal proteins (PubMed:7584149, PubMed:8805247). Peptide-bound HLA-G-B2M complex acts as a ligand for inhibitory/activating KIR2DL4, LILRB1 and LILRB2 receptors on uterine immune cells to promote fetal development while maintaining maternal-fetal tolerance (PubMed:16366734, PubMed:19304799, PubMed:20448110, PubMed:23184984, PubMed:27859042, PubMed:29262349).…
Forms a heterotrimer with B2M and a self-peptide (peptide-bound HLA-G-B2M) (PubMed:7584149, PubMed:8805247). HLA-G-B2M complex interacts with components of the antigen processing machinery TAPBP and TAP1-TAP2 complex; this interaction is required for loading of high affinity peptides and heterotrimer translocation to the cell surface (PubMed:7584149). Interacts with CALCR; this interaction is…
Cell membrane, Endoplasmic reticulum membrane, Early endosome membrane, Secreted, Early endosome, Cell projection, filopodium membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3KYO | X-ray | 1.7 Å | A/C=26-298 |
| 1YDP | X-ray | 1.9 Å | A=26-300 |
| 3KYN | X-ray | 2.4 Å | A=26-299 |
| 2DYP | X-ray | 2.5 Å | A=25-300 |
| 3BZE | X-ray | 2.5 Å | P/Q/R/S=3-11 |
| 6K60 | X-ray | 3.15 Å | A/E=25-300 |
| 2D31 | X-ray | 3.2 Å | A/D=25-300 |
| 6AEE | X-ray | 3.3 Å | A/D=25-300 |
| 3CDG | X-ray | 3.4 Å | P/Q=3-11 |
| 3CII | X-ray | 4.41 Å | C/F=3-11 |
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