P41220: Regulator of G-protein signaling 2 (RGS2)

Regulator of G-protein signaling 2 (RGS2) is a 211-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P41220.

Gene
RGS2
Organism
Homo sapiens
Length
211 residues
Mean pLDDT
80.1
Model
AF-P41220-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.1 (confident 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 accurate60%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:11063746, PubMed:19478087). It is involved in the negative regulation of the angiotensin-activated signaling pathway (PubMed:28784619). Plays a role in the regulation of blood pressure in response to signaling via G protein-coupled receptors and GNAQ. Plays a role in regulating the constriction and relaxation of vascular smooth muscle (By similarity). Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein (PubMed:19736320)

Subunit structure

Interacts with GNAQ (PubMed:18434541, PubMed:19478087, PubMed:28784619). Does not interact with GNAI1 and GNAI3 (PubMed:18434541, PubMed:19478087). Interacts with EIF2B5 (PubMed:19736320). Interacts with PRKG1 (isoform alpha) (PubMed:14608379). Interacts with FBXO44; this interaction mediates RGS2 ubiquitination and subsequent degradation (PubMed:25970626)

Subcellular location

Cell membrane, Cytoplasm, Nucleus, nucleolus, Mitochondrion

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2AF0X-ray2.3 ÅA=71-203
4EKDX-ray2.71 ÅB=72-203
2V4ZX-ray2.8 ÅB=71-209
4EKCX-ray7.4 ÅB/D=72-203

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