Q92574: Hamartin (TSC1)

Hamartin (TSC1) is a 1164-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92574.

Gene
TSC1
Organism
Homo sapiens
Length
1164 residues
Mean pLDDT
62.1
Model
AF-Q92574-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.1 (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 accurate25%
70 to 90Confident: backbone generally right23%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions43%

What pLDDT means and how to read it

Function

Non-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:12906785, PubMed:15340059, PubMed:24529379, PubMed:28215400). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12906785, PubMed:15340059, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing…

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:12906785, PubMed:15963462, PubMed:16464865, PubMed:17658474, PubMed:22795129, PubMed:24529379, PubMed:26893383, PubMed:28215400, PubMed:33215753, PubMed:33436626, PubMed:9580671, PubMed:9809973). Probably forms a…

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
4Z6YX-ray2.81 ÅC/D/F/H=938-993
9CE3EM2.9 ÅC/D=1-1164
5EJCX-ray3.1 ÅC/D/E/F=939-992
9C9IX-ray3.18 ÅB/D/F/H/X=648-681
7DL2EM4.4 ÅC/D=1-1164

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