P15391: B-lymphocyte antigen CD19 (CD19)

B-lymphocyte antigen CD19 (CD19) is a 556-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15391.

Gene
CD19
Organism
Homo sapiens
Length
556 residues
Mean pLDDT
62.2
Model
AF-P15391-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.2 (low 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 accurate24%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions45%

What pLDDT means and how to read it

Function

Functions as a coreceptor for the B-cell antigen receptor complex (BCR) on B-lymphocytes (PubMed:29523808). Decreases the threshold for activation of downstream signaling pathways and for triggering B-cell responses to antigens (PubMed:1373518, PubMed:16672701, PubMed:2463100). Activates signaling pathways that lead to the activation of phosphatidylinositol 3-kinase and the mobilization of intracellular Ca(2+) stores (PubMed:12387743, PubMed:16672701, PubMed:9317126, PubMed:9382888). Is not required for early steps during B cell differentiation in the blood marrow (PubMed:9317126). Required for normal differentiation of B-1 cells (By similarity). Required for normal B cell differentiation…

Subunit structure

Interacts with CR2/CD21 (PubMed:1702139). Part of a complex composed of CD19, CR2/CD21, CD81 and IFITM1/CD225 in the membrane of mature B-cells (PubMed:1383329). Interacts directly with CD81 (via the second extracellular domain); this interaction is initiated early during biosynthesis in the ER/pre-Golgi compartments and is essential for trafficking and compartmentalization of CD19 receptor on…

Subcellular location

Cell membrane, Membrane raft

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6AL5X-ray3.0 ÅA=21-277
7URVEM3.05 ÅC=21-277
7URXEM3.4 ÅC=1-278
7JICEM3.8 ÅA=20-327

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