P20273: B-cell receptor CD22 (CD22)

B-cell receptor CD22 (CD22) is a 847-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P20273.

Gene
CD22
Organism
Homo sapiens
Length
847 residues
Mean pLDDT
79.4
Model
AF-P20273-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.4 (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 accurate51%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions18%

What pLDDT means and how to read it

Function

Most highly expressed siglec (sialic acid-binding immunoglobulin-like lectin) on B-cells that plays a role in various aspects of B-cell biology including differentiation, antigen presentation, and trafficking to bone marrow (PubMed:34330755, PubMed:8627166). Binds to alpha 2,6-linked sialic acid residues of surface molecules such as CD22 itself, CD45 and IgM in a cis configuration. Can also bind to ligands on other cells as an adhesion molecule in a trans configuration (PubMed:20172905). Acts as an inhibitory coreceptor on the surface of B-cells and inhibits B-cell receptor induced signaling, characterized by inhibition of the calcium mobilization and cellular activation. Mechanistically,…

Subunit structure

Predominantly monomer of isoform CD22-beta. Also found as heterodimer of isoform CD22-beta and a shorter isoform. Interacts with PTPN6/SHP-1, LYN, SYK, PIK3R1/PIK3R2 and PLCG1 upon phosphorylation. Interacts with GRB2, INPP5D and SHC1 upon phosphorylation (By similarity). May form a complex with INPP5D/SHIP, GRB2 and SHC1

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5VKJX-ray2.12 ÅA=20-330
5VKMX-ray2.2 ÅA=20-330
7O52X-ray2.41 ÅU=504-687
9ROBX-ray2.7 ÅA/B=20-330
9RM3X-ray2.86 ÅA/B/C/D=20-330
5VL3X-ray3.1 ÅQ/R/S/T=22-330
9RO7X-ray3.15 ÅA/B/C/D=20-330

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