Q6R327: Rapamycin-insensitive companion of mTOR (RICTOR)

Rapamycin-insensitive companion of mTOR (RICTOR) is a 1708-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6R327.

Gene
RICTOR
Organism
Homo sapiens
Length
1708 residues
Mean pLDDT
65.9
Model
AF-Q6R327-F1 v6
Model created
1 Aug 2025
PDB structures
16

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Model confidence (pLDDT)

The mean pLDDT of this model is 65.9 (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 accurate27%
70 to 90Confident: backbone generally right33%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions36%

What pLDDT means and how to read it

Function

Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex,…

Subunit structure

Component of the mechanistic target of rapamycin complex 2 (mTORC2), consisting in two heterotretramers composed of MTOR, MLST8, RICTOR and MAPKAP1/SIN1 (PubMed:15268862, PubMed:15467718, PubMed:17461779, PubMed:17599906, PubMed:29424687, PubMed:29567957, PubMed:33158864, PubMed:34519268, PubMed:35926713). The mTORC2 core complex associates with PRR5/PROTOR1 and/or PRR5L/PROTOR2…

Subcellular location

Cell membrane, Endoplasmic reticulum membrane, Lysosome membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9T94EM2.6 ÅE=1-1708
9ZBKEM2.6 ÅC=25-1694
9T93EM2.86 ÅE=1-1708
6ZWOEM3.0 ÅF=1-1708
9T7JEM3.0 ÅE/F=1-1708
9TDTEM3.0 ÅE=1-1708
9T92EM3.1 ÅE/F=1-1708
6ZWMEM3.2 ÅE/F=1-1708
7PE8EM3.2 ÅE=1-1708
9ZBJEM3.2 ÅC=23-1694
7TZOEM3.28 ÅE/F=1-1708
9TDSEM3.3 ÅE/F=1-1708
7PE7EM3.41 ÅE/F=1-1708
7PE9EM3.7 ÅE=1-1708
5ZCSEM4.9 ÅE/F=1-1018
9TPWEM6.4 ÅE/F=1-1708

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