P20023: Complement receptor type 2 (CR2)

Complement receptor type 2 (CR2) is a 1033-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P20023.

Gene
CR2
Organism
Homo sapiens
Length
1033 residues
Mean pLDDT
74.9
Model
AF-P20023-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.9 (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 accurate2%
70 to 90Confident: backbone generally right71%
50 to 70Low: treat with caution21%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Serves as a receptor for various ligands including complement component CD3d, HNRNPU OR IFNA1 (PubMed:1849076, PubMed:21527715, PubMed:7753047). When C3d is bound to antigens, attaches to C3d on B-cell surface and thereby facilitates the recognition and uptake of antigens by B-cells (PubMed:21527715). This interaction enhances B-cell activation and subsequent immune responses. Forms a complex with several partners on the surface of B-cells including CD19, FCRL5 and CD81, to form the B-cell coreceptor complex that plays a crucial role in B-cell activation and signaling (PubMed:1383329, PubMed:30107486). Also induces specific intracellular signaling separately from the BCR and CD19 by…

Subunit structure

Interacts (via Sushi domain 1 and 2) with C3 (PubMed:11387479, PubMed:21527715). Interacts with CD19 (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 (via Sushi domain 1 and 2) with FCER2 (via the C-terminus). Interacts with CD23 (PubMed:1386409). Interacts with FCRL5 (PubMed:30107486). Interacts…

Subcellular location

Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8SM0X-ray1.68 ÅC=21-149
1LY2X-ray1.8 ÅA=22-148
1GHQX-ray2.04 ÅB/C=21-153
3OEDX-ray3.16 ÅC/D=19-153
8ZNIEM3.29 ÅA=1-971
1W2RX-rayA=20-153
1W2SX-rayB=20-153
2ATYX-rayA/B=21-153
2GSXX-rayA=21-971

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