Immunoglobulin heavy constant gamma 4 (IGHG4) is a 396-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P01861.
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The mean pLDDT of this model is 86.8 (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 | 69% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 12% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Constant region of immunoglobulin (Ig) heavy chains. Igs are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound Igs serve as receptors, which upon binding to a specific antigen trigger the clonal expansion and differentiation of B lymphocytes into Ig-secreting plasma cells. Secreted Igs known as antibodies mediate the effector phase of humoral immunity by blocking the interaction of infectious antigens with cellular receptors (via the antigen-binding region) and eliciting effector mechanisms that lead to pathogen neutralization (via the constant region) (PubMed:17576170, PubMed:20176268, PubMed:22158414). The…
Immunoglobulins (Igs) are composed of two identical heavy chains and two identical light chains; disulfide-linked. Ig-gamma 4 (IgG4) molecules can oligomerize (via non-covalent Fc region interactions) to form hexameric rings that serve as platforms for binding of the C1 complex (PubMed:33563762). Assembled in immune complexes interacts (via Fc region and its N-linked glycan) with FCGR1A, FCGR2A,…
Secreted, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4B53 | X-ray | 1.8 Å | A/B=222-325 |
| 5W5N | X-ray | 1.85 Å | A/B=106-325 |
| 4C54 | X-ray | 1.9 Å | A/B=114-325 |
| 5W5M | X-ray | 1.9 Å | A/B=106-325 |
| 5HVW | X-ray | 1.95 Å | A=115-324 |
| 6WMH | X-ray | 2.3 Å | A/H=118-324 |
| 4C55 | X-ray | 2.35 Å | A/B=110-325 |
| 6WNA | X-ray | 2.4 Å | H=118-324 |
| 6WOL | X-ray | 2.49 Å | H=117-325 |
| 6WIB | X-ray | 2.55 Å | A=115-325 |
| 4D2N | X-ray | 2.7 Å | A/B/C/D=102-325 |
| 5LG1 | X-ray | 2.7 Å | A/B=114-325 |
| 2FL5 | X-ray | 3.0 Å | B/D/F/H=1-99 |
| 1BBJ | X-ray | 3.1 Å | B/H=1-98 |
| 3EO1 | X-ray | 3.1 Å | B/E/H/K=1-105 |
| 1ADQ | X-ray | 3.15 Å | A=118-323 |
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