P07101: Tyrosine 3-monooxygenase (TH)

Tyrosine 3-monooxygenase (TH) is a 528-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07101.

Gene
TH
Organism
Homo sapiens
Length
528 residues
Mean pLDDT
80.8
Model
AF-P07101-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.8 (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 accurate58%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions17%

What pLDDT means and how to read it

Function

Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of catecholamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (PubMed:15287903, PubMed:1680128, PubMed:17391063, PubMed:24753243, PubMed:34922205, PubMed:8528210, Ref.18). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity)

Subunit structure

Homotetramer (PubMed:24947669, Ref.18). Interacts (when phosphorylated at Ser-19) with YWHAG; one YWHAG dimer binds to one TH tetramer and this interaction may influence the phosphorylation and dephosphorylation of other sites (PubMed:24947669). Interacts with NT5DC2; the interaction results in reduced phosphorylation and decreased catalytic activity of TH (By similarity)

Subcellular location

Cytoplasm, perinuclear region, Nucleus, Cell projection, axon, Cytoplasm, Cytoplasmic vesicle, secretory vesicle, synaptic vesicle

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2XSNX-ray2.68 ÅA/B/C/D=193-528
4J6SX-ray3.08 ÅE/F/G/H=1-74
6ZZUEM3.5 ÅA/B/C/D=194-528
6ZVPEM4.0 ÅA/B/C/D=71-528
7A2GEM4.1 ÅA/B/C/D=109-528
6ZN2EM4.3 ÅA/C/E/G=194-528, B/D/F/H=71-88
7PIMEM4.6 ÅA/B/D/F=194-528, C/E/G/H=71-88

More AlphaFold highlights

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