P10599: Thioredoxin (TXN)

Thioredoxin (TXN) is a 105-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P10599.

Gene
TXN
Organism
Homo sapiens
Length
105 residues
Mean pLDDT
97.6
Model
AF-P10599-F1 v6
Model created
1 Aug 2025
PDB structures
37

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 97.6 (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 accurate99%
70 to 90Confident: backbone generally right1%
50 to 70Low: treat with caution0%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:17182577, PubMed:19032234, PubMed:2176490). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity (PubMed:16408020, PubMed:17606900). Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity…

Subunit structure

Homodimer; disulfide-linked (PubMed:17260951, PubMed:9369469). Interacts with TXNIP through the redox-active site (PubMed:17260951). Interacts with MAP3K5 and CASP3 (PubMed:15246877). In case of infection, interacts with S.typhimurium protein slrP (PubMed:19690162). Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity in a redox-dependent manner (PubMed:9108029)

Subcellular location

Nucleus, Cytoplasm, Secreted

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4OO4X-ray0.97 ÅA/B=1-105
3M9JX-ray1.1 ÅA/B=1-105
2IFQX-ray1.2 ÅA/B/C=1-105
2HSHX-ray1.35 ÅA=1-105
5DQYX-ray1.4 ÅA=1-105
3M9KX-ray1.5 ÅA/B=1-105
4OO5X-ray1.54 ÅA=1-105
1ERVX-ray1.65 ÅA=1-105
2HXKX-ray1.65 ÅA/B/C=1-105
1ERTX-ray1.7 ÅA=1-105
2IIYX-ray1.7 ÅA=1-105
3KD0X-ray1.7 ÅA=1-105
1ERWX-ray1.8 ÅA=1-105
4POMX-ray1.85 ÅA/B/C/D=1-105
1AIUX-ray2.0 ÅA=1-105
4LL1X-ray2.0 ÅB/D=1-105
3E3EX-ray2.01 ÅA/B=1-105
1AUCX-ray2.1 ÅA=1-105
1ERUX-ray2.1 ÅA=1-105
3QFAX-ray2.2 ÅC/D=2-105

Showing 20 of 37 experimental structures (best resolution first).

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.