P01876: Immunoglobulin heavy constant alpha 1 (IGHA1)

Immunoglobulin heavy constant alpha 1 (IGHA1) is a 398-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P01876.

Gene
IGHA1
Organism
Homo sapiens
Length
398 residues
Mean pLDDT
81.9
Model
AF-P01876-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.9 (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 accurate51%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light…

Subunit structure

Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked (PubMed:20176268). Monomeric or polymeric (PubMed:2241915). Part of the secretory IgA (sIgA) complex that consists of two, four or five IgA monomers, and two additional non-Ig polypeptides, namely the JCHAIN and the secretory component (the proteolytic product of PIGR)

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
9R2EX-ray2.54 ÅP/Q=123-333
9OFRX-ray2.65 ÅA/B/E/G=123-333
6UE7EM2.9 ÅA/B/F/G=123-333
1OW0X-ray3.1 ÅA/B=122-333
8SKVEM3.1 ÅA/B/C/D=1-333
6LX3EM3.15 ÅA/B/C/D=122-333
2QEJX-ray3.2 ÅA/B=123-333
8SKUEM3.2 ÅA/B/C/D=1-333
6LXWEM3.27 ÅA/B/C/D=122-333
7UVLEM3.56 ÅA/B=123-331
6XJAEM4.0 ÅA/B=122-331
1IGAX-rayA/B=1-333
2ESGX-rayA/B=1-333
3CHNX-rayA/B/C/D=1-333

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