P01871: Immunoglobulin heavy constant mu (IGHM)

Immunoglobulin heavy constant mu (IGHM) is a 474-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P01871.

Gene
IGHM
Organism
Homo sapiens
Length
474 residues
Mean pLDDT
85.4
Model
AF-P01871-F1 v6
Model created
1 Aug 2025
PDB structures
31

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 85.4 (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 accurate53%
70 to 90Confident: backbone generally right35%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions4%

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

The basic structural unit of both sIgM and mIgM molecules consists of two identical heavy chains and two identical light chains; disulfide-linked. N-terminal variable regions of the heavy and light chains form the antigen binding sites, whereas the C-terminal constant regions of the heavy chains interact with immune receptors to mediate effector functions

Subcellular location

Secreted, Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2AGJX-ray2.6 ÅH=1-106
1HEZX-ray2.7 ÅB/D=1-104
8BPGEM3.1 ÅC/D/E/F=106-433
9UO3EM3.17 ÅA/B/C/D/E/F/G/H/I/J/K/L=106-433
7YSGEM3.18 ÅA/B/C/D/E/F/G/H/K/L=222-433
9UO4EM3.29 ÅA/B/C/D/E/F/G/H/I/J/K/L=106-433
7K0CEM3.3 ÅA/B/E/F/G/H/I/J/K/L=103-433
7XQ8EM3.3 ÅC/v=1-474
7YG2EM3.32 ÅA/B/C/D/E/F/G/H/K/L=106-433
7YTCEM3.39 ÅA/B/C/D/E/F/G/H/K/L=222-433
8WYREM3.39 ÅA/B/C/D/E/F/G/H/K/L=106-433
6KXSEM3.4 ÅA/B/C/D/E/F/G/H/K/L=106-433
8WYSEM3.41 ÅA/L=106-433
8BPFEM3.5 ÅA/B/C/D/E/F/G/H/K/L=106-433
7Y0HEM3.56 ÅA/B/C/D/E/F/G/H/K/L=106-433
8R83EM3.57 ÅA/B/C/D/E/F/G/H/K/L=106-433
7QDOEM3.6 ÅA/B=105-446
8GZNEM3.6 ÅA/B/C/D/E/F/G/H/K/L=1-433
8R84EM3.6 ÅA/B/K/L=106-433
9ARVEM3.6 ÅA/B/C/D/E/L/M/N/O/P=106-433

Showing 20 of 31 experimental structures (best resolution first).

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.