P01861: Immunoglobulin heavy constant gamma 4 (IGHG4)

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.

Gene
IGHG4
Organism
Homo sapiens
Length
396 residues
Mean pLDDT
86.8
Model
AF-P01861-F1 v6
Model created
1 Aug 2025
PDB structures
16

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Model confidence (pLDDT)

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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate69%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

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…

Subunit structure

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,…

Subcellular location

Secreted, Cell membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
4B53X-ray1.8 ÅA/B=222-325
5W5NX-ray1.85 ÅA/B=106-325
4C54X-ray1.9 ÅA/B=114-325
5W5MX-ray1.9 ÅA/B=106-325
5HVWX-ray1.95 ÅA=115-324
6WMHX-ray2.3 ÅA/H=118-324
4C55X-ray2.35 ÅA/B=110-325
6WNAX-ray2.4 ÅH=118-324
6WOLX-ray2.49 ÅH=117-325
6WIBX-ray2.55 ÅA=115-325
4D2NX-ray2.7 ÅA/B/C/D=102-325
5LG1X-ray2.7 ÅA/B=114-325
2FL5X-ray3.0 ÅB/D/F/H=1-99
1BBJX-ray3.1 ÅB/H=1-98
3EO1X-ray3.1 ÅB/E/H/K=1-105
1ADQX-ray3.15 ÅA=118-323

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