P0CF51: T cell receptor gamma constant 1 (TRGC1)

T cell receptor gamma constant 1 (TRGC1) is a 173-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0CF51.

Gene
TRGC1
Organism
Homo sapiens
Length
173 residues
Mean pLDDT
86.6
Model
AF-P0CF51-F1 v6
Model created
1 Aug 2025
PDB structures
19

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 86.6 (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 accurate68%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions5%

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
4LFHX-ray2.3 ÅG=1-122
4LHUX-ray2.87 ÅG=1-122
9CI8EM3.01 Ån=128-165
8JBVEM3.02 ÅN/n=1-173
9JY1EM3.08 ÅN/n=1-173
9JY2EM3.24 Ån=127-164
9JY4EM3.29 ÅN/n=1-173
9JXZEM3.31 Ån=1-173
9JY3EM3.35 ÅN/n=127-164
9CIAEM3.39 Ån=128-163
8JC0EM3.4 Ån=1-173
9JY0EM3.69 Ån=1-173
8WY0EM3.8 Ån=1-173
8WYIEM3.9 Ån=1-173
9J5MEM3.94 ÅB/I=1-109
8WXEEM4.0 Ån=1-173
9J5JEM4.05 ÅB/I=1-109
8YC0EM4.12 Ån=1-173
8JCBEM9.5 ÅN/n=1-173

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.