P10747: T-cell-specific surface glycoprotein CD28 (CD28)

T-cell-specific surface glycoprotein CD28 (CD28) is a 220-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P10747.

Gene
CD28
Organism
Homo sapiens
Length
220 residues
Mean pLDDT
81.3
Model
AF-P10747-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.3 (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 right18%
50 to 70Low: treat with caution30%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Receptor that plays a role in T-cell activation, proliferation, survival and the maintenance of immune homeostasis (PubMed:1650475, PubMed:7568038). Functions not only as an amplifier of TCR signals but delivers unique signals that control intracellular biochemical events that alter the gene expression program of T-cells (PubMed:24665965). Stimulation upon engagement of its cognate ligands CD80 or CD86 increases proliferation and expression of various cytokines in particular IL2 production in both CD4(+) and CD8(+) T-cell subsets (PubMed:12196291, PubMed:1650475, PubMed:35397202). Mechanistically, ligation induces recruitment of protein kinase C-theta/PRKCQ and GRB2 leading to NF-kappa-B…

Subunit structure

Homodimer; disulfide-linked (PubMed:35397202). Interacts with DUSP14. Binds to CD80/B7-1 and CD86/B7-2/B70 (PubMed:12196291). Interacts with GRB2 (PubMed:24098653, PubMed:7568038). Interacts with PIK3R1 (PubMed:7568038). Interacts with PRKCQ (PubMed:21964608)

Subcellular location

Cell membrane, Cell surface

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5GJIX-ray0.9 ÅB=189-196
5AULX-ray1.1 ÅB=189-196
5GJHX-ray1.2 ÅB/D=189-196
3WA4X-ray1.35 ÅB=189-196
7PPNX-ray1.9 ÅB=183-198
1YJDX-ray2.7 ÅC=17-152
8S6ZX-ray3.05 ÅC/F=19-152
6O8DX-ray3.55 ÅC=19-136
7VU5NMRA/B=148-188
8W2VNMRA=114-152

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