B7Z8K6: T cell receptor delta constant (TRDC)

T cell receptor delta constant (TRDC) is a 153-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: B7Z8K6.

Gene
TRDC
Organism
Homo sapiens
Length
153 residues
Mean pLDDT
81.4
Model
AF-B7Z8K6-F1 v6
Model created
1 Aug 2025
PDB structures
12

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.4 (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 accurate63%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

Constant region of T cell receptor (TR) delta 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
9CI8EM3.01 Åm=118-153
8JBVEM3.02 ÅM/m=1-153
1HXMX-ray3.12 ÅA/C/E/G=1-109
9JY2EM3.24 Åm=117-152
9JY3EM3.35 ÅM/m=117-152
9CIAEM3.39 Åm=118-152
8JC0EM3.4 Åm=1-153
8WY0EM3.8 Åm=1-153
8WYIEM3.9 Åm=1-133
8WXEEM4.0 Åm=1-153
8YC0EM4.12 Åm=1-153
8JCBEM9.5 ÅM/m=1-153

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