A0A0B4J279: T cell receptor alpha variable 21 (TRAV21)

T cell receptor alpha variable 21 (TRAV21) is a 112-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: A0A0B4J279.

Gene
TRAV21
Organism
Homo sapiens
Length
112 residues
Mean pLDDT
92.8
Model
AF-A0A0B4J279-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.8 (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 right18%
50 to 70Low: treat with caution4%
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) alpha chain that participates in the antigen recognition (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling…

Subunit structure

Alpha-beta TR is a heterodimer composed of an alpha and beta chain; disulfide-linked. The alpha-beta TR is associated with the transmembrane signaling CD3 coreceptor proteins to form the TR-CD3 (TcR or 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
4WW1X-ray1.38 ÅA=20-110
2BNUX-ray1.4 ÅA=21-112
2BNQX-ray1.7 ÅD=21-112
2BNRX-ray1.9 ÅD=21-112
5EU6X-ray2.02 ÅD=20-111
5BS0X-ray2.4 ÅD=21-112
4WW2X-ray2.48 ÅA=20-110
6Q3SX-ray2.5 ÅD=21-112
5BRZX-ray2.62 ÅD=21-112

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