Q96B36: Proline-rich AKT1 substrate 1 (AKT1S1)

Proline-rich AKT1 substrate 1 (AKT1S1) is a 256-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96B36.

Gene
AKT1S1
Organism
Homo sapiens
Length
256 residues
Mean pLDDT
66.9
Model
AF-Q96B36-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 66.9 (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 accurate17%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution32%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

Negative regulator of the mechanistic target of rapamycin complex 1 (mTORC1), an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:17277771, PubMed:17386266, PubMed:17510057, PubMed:29236692). In absence of insulin and nutrients, AKT1S1 associates with the mTORC1 complex and directly inhibits mTORC1 activity by blocking the MTOR substrate-recruitment site (PubMed:29236692). In response to insulin and nutrients, AKT1S1 dissociates from mTORC1 (PubMed:17386266, PubMed:18372248). Its activity is dependent on its phosphorylation state and binding to 14-3-3…

Subunit structure

Associated component of the mechanistic target of rapamycin complex 1 (mTORC1), which contains core MTOR, MLST8 and RPTOR (PubMed:17277771, PubMed:17386266, PubMed:17510057, PubMed:29236692, PubMed:31601764). Dissociates from mTORC1 in response to insulin treatment (PubMed:17386266, PubMed:18372248). mTORC1 binds to and is inhibited by FKBP12-rapamycin (PubMed:17277771, PubMed:31601764).…

Subcellular location

Cytoplasm, cytosol

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5WBYX-ray3.1 ÅO/P=114-207
5WBLX-ray3.35 ÅT=124-139
5WBUX-ray3.42 ÅO/P/Q/R=173-256
6SB0EM5.5 ÅO/T=1-256

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