A0A1B0GX56: T cell receptor delta variable 1 (TRDV1)

T cell receptor delta variable 1 (TRDV1) is a 115-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: A0A1B0GX56.

Gene
TRDV1
Organism
Homo sapiens
Length
115 residues
Mean pLDDT
90.7
Model
AF-A0A1B0GX56-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 90.7 (very high 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 accurate79%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution17%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

V region of the variable domain 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…

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
7RYLX-ray2.0 ÅD=20-115
7RYNX-ray2.7 ÅD=20-115
7RYOX-ray3.0 ÅD=20-115
8JBVEM3.02 ÅM/m=21-114
7RYMX-ray3.2 ÅD=20-115
8WXEEM4.0 Åm=16-114
8JCBEM9.5 ÅM/m=21-114

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