A0A0K0K1A5: T cell receptor beta variable 6-5 (TRBV6-5)

T cell receptor beta variable 6-5 (TRBV6-5) is a 114-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: A0A0K0K1A5.

Gene
TRBV6-5
Organism
Homo sapiens
Length
114 residues
Mean pLDDT
91.9
Model
AF-A0A0K0K1A5-F1 v6
Model created
1 Aug 2025
PDB structures
18

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.9 (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 accurate82%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution15%
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) beta 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 the…

Subunit structure

Alpha-beta TR is a heterodimer composed of an alpha and beta chain; disulfide-linked (PubMed:26875526). 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,…

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2BNUX-ray1.4 ÅB=22-114
2BNQX-ray1.7 ÅE=22-114
2BNRX-ray1.9 ÅE=22-114
8RLTX-ray2.25 ÅE/J=20-112
8RLUX-ray2.35 ÅE/J=20-112
1BD2X-ray2.5 ÅE=20-114
6Q3SX-ray2.5 ÅE=22-114
5E9DX-ray2.51 ÅE/J=20-112
1AO7X-ray2.6 ÅE=20-114
8RLVX-ray2.61 ÅE/J=20-112
5MENX-ray2.81 ÅE=21-114
7FJEEM3.0 Ån=1-112
4WWKX-ray3.1 ÅB=19-113
7FJFEM3.1 Ån=1-112
8TW6EM3.1 ÅB=2-114
7FJDEM3.2 Ån=1-112
8TW4EM3.3 ÅB=2-114
6JXREM3.7 Ån=23-112

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