Q9P0N9: TBC1 domain family member 7 (TBC1D7)

TBC1 domain family member 7 (TBC1D7) is a 293-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9P0N9.

Gene
TBC1D7
Organism
Homo sapiens
Length
293 residues
Mean pLDDT
92.7
Model
AF-Q9P0N9-F1 v6
Model created
1 Aug 2025
PDB structures
6

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 92.7 (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 accurate89%
70 to 90Confident: backbone generally right2%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions4%

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:22795129, PubMed:24529379). 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:22795129, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1)…

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:17658474, PubMed:22795129, PubMed:24529379, PubMed:33436626). Interacts with TSC1 (via C-terminal half of the coiled-coil domain) (PubMed:17658474, PubMed:26893383)

Subcellular location

Lysosome membrane, Cytoplasmic vesicle, Cytoplasm, cytosol

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3QWLX-ray1.9 ÅA=1-293
5ULOX-ray2.14 ÅC/D=115-126
4Z6YX-ray2.81 ÅA/B/E/G=21-293
9CE3EM2.9 ÅE=1-293
5EJCX-ray3.1 ÅA/B=18-293
7DL2EM4.4 ÅE=21-287

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.