P49815: Tuberin (TSC2)

Tuberin (TSC2) is a 1807-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P49815.

Gene
TSC2
Organism
Homo sapiens
Length
1807 residues
Mean pLDDT
67.9
Model
AF-P49815-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 67.9 (low 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 accurate13%
70 to 90Confident: backbone generally right51%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions30%

What pLDDT means and how to read it

Function

Catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12842888, PubMed:12906785, PubMed:15340059, PubMed:22819219, PubMed:24529379, PubMed:28215400, PubMed:33436626, PubMed:35772404). Within the TSC-TBC complex, TSC2 acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12172553, PubMed:12820960, PubMed:12842888,…

Subunit structure

Component of the TSC-TBC complex (also named Rhebulator complex), composed of 2 molecules of TSC1, 2 molecules of TSC2 and 1 molecule of TBC1D7 (PubMed:10585443, PubMed:12172553, PubMed:12842888, PubMed:12906785, PubMed:15963462, PubMed:22795129, PubMed:24529379, PubMed:28215400, PubMed:33436626, PubMed:9580671). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones…

Subcellular location

Lysosome membrane, Cytoplasm, cytosol

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9CE3EM2.9 ÅA/B=2-1807
7DL2EM4.4 ÅA/B=50-1807

More AlphaFold highlights

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