P0DTU4: T cell receptor beta chain MC.7.G5 (TRB)

T cell receptor beta chain MC.7.G5 (TRB) is a 315-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0DTU4.

Gene
TRB
Organism
Homo sapiens
Length
315 residues
Mean pLDDT
88.9
Model
AF-P0DTU4-F1 v6
Model created
1 Aug 2025
PDB structures
12

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.9 (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 accurate77%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

The beta 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 intracellular…

Subunit structure

Disulfide-linked heterodimer with TRAV38-2DV8*01J31*01C*01 alpha 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…

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8YIVX-ray2.1 ÅE=19-266
8RLTX-ray2.25 ÅE/J=113-266
8YJ2X-ray2.26 ÅE=19-266
8RLUX-ray2.35 ÅE/J=113-266
8RLVX-ray2.61 ÅE/J=113-266
8T4ZX-ray2.69 ÅD=137-266
9HI7X-ray2.81 ÅE/I=19-266
8TW6EM3.1 ÅB=132-315
8TW4EM3.3 ÅB=132-315
8Y6XX-ray3.4 ÅE=20-266
8YJ3X-ray3.5 ÅA/C/E/G=19-266
9C3EEM3.5 ÅB=1-315

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