P03986: T cell receptor gamma constant 2 (TRGC2)

T cell receptor gamma constant 2 (TRGC2) is a 189-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P03986.

Gene
TRGC2
Organism
Homo sapiens
Length
189 residues
Mean pLDDT
82.1
Model
AF-P03986-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.1 (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 accurate62%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Constant region of T cell receptor (TR) gamma chain that participates in the antigen recognition (PubMed:24600447). Gamma-delta TRs recognize a variety of self and foreign non-peptide antigens frequently expressed at the epithelial boundaries between the host and external environment, including endogenous lipids presented by MH-like protein CD1D and phosphoantigens presented by butyrophilin-like molecule BTN3A1. Upon antigen recognition induces rapid, innate-like immune responses involved in pathogen clearance and tissue repair (PubMed:23348415, PubMed:28920588). Binding of gamma-delta TR complex to antigen triggers phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs)…

Subunit structure

Gamma-delta TR is a heterodimer composed of a gamma and delta chain; disulfide-linked. The gamma-delta TR is associated with the transmembrane signaling CD3 coreceptor proteins following the stoichiometry: a single gamma-delta TR heterodimer associates with one CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer and one CD247 homodimer forming a stable octameric structure. Upon activation,…

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1HXMX-ray3.12 ÅB/D/F/H=1-120

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