Immunoglobulin heavy constant gamma 1 (IGHG1) is a 399-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P01857.
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The mean pLDDT of this model is 86.7 (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 | 14% |
| Below 50 | Very low: often disordered regions | 4% |
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 (PubMed:20176268). Ig-gamma 1 (IgG1) molecules oligomerize (via non-covalent Fc region interactions) to form hexameric rings that serve as platforms for binding of the C1 complex (PubMed:33563762). Interacts (via Fc region and its N-linked glycan) with Fc receptors (via D2 domain).…
Secreted, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4LLD | X-ray | 1.19 Å | A=1-103 |
| 3TV3 | X-ray | 1.29 Å | H=1-104 |
| 4LLQ | X-ray | 1.42 Å | A=1-103 |
| 5HSF | X-ray | 1.52 Å | A/B=221-343 |
| 6YT7 | X-ray | 1.55 Å | B=104-328 |
| 4NWU | X-ray | 1.6 Å | H=1-105 |
| 1L6X | X-ray | 1.65 Å | A=120-326 |
| 3TWC | X-ray | 1.65 Å | H=1-104 |
| 5JIH | X-ray | 1.66 Å | A/B=108-328 |
| 3MCL | X-ray | 1.7 Å | H=1-107 |
| 5U66 | X-ray | 1.7 Å | A=120-326 |
| 3DJ9 | X-ray | 1.75 Å | A=119-225 |
| 4BSV | X-ray | 1.75 Å | A/B=106-328 |
| 4LLM | X-ray | 1.75 Å | A=1-103 |
| 4NWT | X-ray | 1.75 Å | H=1-105 |
| 6N35 | X-ray | 1.75 Å | H/M=1-101 |
| 4XMP | X-ray | 1.78 Å | H=1-103 |
| 5JII | X-ray | 1.79 Å | A/B=108-328 |
| 1N7M | X-ray | 1.8 Å | L=1-102 |
| 4W4N | X-ray | 1.8 Å | A/B=107-328 |
Showing 20 of 216 experimental structures (best resolution first).
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