Q9HB90: Ras-related GTP-binding protein C (RRAGC)

Ras-related GTP-binding protein C (RRAGC) is a 399-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HB90.

Gene
RRAGC
Organism
Homo sapiens
Length
399 residues
Mean pLDDT
68.8
Model
AF-Q9HB90-F1 v6
Model created
1 Aug 2025
PDB structures
21

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.8 (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 accurate7%
70 to 90Confident: backbone generally right54%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade (PubMed:20381137, PubMed:24095279, PubMed:27234373, PubMed:31601708, PubMed:31601764, PubMed:32612235, PubMed:34071043, PubMed:36697823, PubMed:37057673). Forms heterodimeric Rag complexes with RagA/RRAGA or RagB/RRAGB and cycles between an inactive GTP-bound and an active GDP-bound form: RagC/RRAGC is in its active form when GDP-bound RagC/RRAGC forms a complex with GTP-bound RagA/RRAGA (or RagB/RRAGB) and in an inactive form when GTP-bound RagC/RRAGC heterodimerizes with GDP-bound RagA/RRAGA (or RagB/RRAGB) (PubMed:24095279,…

Subunit structure

Forms a heterodimer with RRAGA, in a sequence-independent manner, and RRAGB (PubMed:11073942, PubMed:14660641, PubMed:32868926). Heterodimerization stabilizes proteins of the heterodimer (PubMed:11073942). The GDP-bound form of RRAGC (in complex with the GTP-bound form of RRAGA or RRAGB), interacts with RPTOR, thereby promoting recruitment of mTORC1 to the lysosomes (PubMed:18497260,…

Subcellular location

Cytoplasm, Nucleus, Lysosome membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3LLUX-ray1.4 ÅA=60-237
6S6DX-ray2.5 ÅC/D=1-399
6S6AX-ray2.63 ÅC/D=1-399
6EHRX-ray2.9 ÅG=239-399
7UX2EM2.9 ÅC/J=1-399
6U62EM3.18 ÅC=2-399
6WJ2EM3.2 ÅG=1-399
7UXCEM3.2 ÅE/L=1-399
7UXHEM3.2 ÅG/N/W/d=1-399
9ED4EM3.23 ÅE/V=1-399
6ULGEM3.31 ÅG=1-399
8DHBEM3.53 ÅA=1-399
6NZDEM3.6 ÅG=1-399
6WJ3EM3.9 ÅG=1-399
7T3BEM3.9 ÅE=1-399
9ED6EM3.98 ÅC=1-399
6CESEM4.0 ÅC=1-399
7T3AEM4.0 ÅL=1-399
7T3CEM4.0 ÅE/L=1-399
6SB0EM5.5 ÅD/J=1-399

Showing 20 of 21 experimental structures (best resolution first).

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