P0DTU3: T cell receptor alpha chain MC.7.G5 (TRA)

T cell receptor alpha chain MC.7.G5 (TRA) is a 275-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0DTU3.

Gene
TRA
Organism
Homo sapiens
Length
275 residues
Mean pLDDT
90.7
Model
AF-P0DTU3-F1 v6
Model created
1 Aug 2025
PDB structures
4

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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 accurate78%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

The alpha chain of TRAV38-2DV8*01J31*01C*01/TRBV25-1*01J2S3*01C2*01 alpha-beta T cell receptor (TR) clonotype that displays pan-cancer cell recognition via the invariant MR1 molecule. On CD8-positive T cell clone MC.7.G5, likely recognizes tumor-specific or -associated metabolite(s) essential for cancer cell survival, triggering killing of many cancer cell types including lung, melanoma, leukemia, colon, breast, prostate, bone and ovarian cancer cells. Mediates cancer cell cytotoxicity in an HLA-independent manner. Has no reactivity to healthy cells, even stressed or infected by bacteria (PubMed:31959982). Antigen recognition initiates TR-CD3 clustering on the cell surface and…

Subunit structure

Disulfide-linked heterodimer with TRBV25-1*01J2S3*01C2*01 beta chain (PubMed:31959982). The alpha-beta TR associates with the transmembrane signaling CD3 coreceptor proteins to form the TR-CD3 (TCR). The assembly of alpha-beta TR heterodimers with CD3 occurs in the endoplasmic reticulum where a single alpha-beta TR heterodimer associates with one CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer…

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8RLTX-ray2.25 ÅD/I=115-220
8RLUX-ray2.35 ÅD/I=115-220
8RLVX-ray2.61 ÅD/I=115-220
9HI7X-ray2.81 ÅD/H=20-220

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