Q5JWF2: Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas (GNAS)

Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas (GNAS) is a 1037-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5JWF2.

Gene
GNAS
Organism
Homo sapiens
Length
1037 residues
Mean pLDDT
56.7
Model
AF-Q5JWF2-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 56.7 (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 right9%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions62%

What pLDDT means and how to read it

Function

Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP. GNAS functions…

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts through its N-terminal region with ALEX which is produced from the same locus in a different open reading frame. This interaction may inhibit its adenylyl cyclase-stimulating activity (By similarity). Interacts with MAGED2 (PubMed:27120771). Interacts with FSHR…

Subcellular location

Cell membrane, Apical cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9BKKEM2.51 ÅA=847-1037
8WW2EM2.79 ÅA=683-1037
8I2GEM2.8 ÅA=848-1037
9DQJEM2.9 ÅB=847-989, B=991-1000, B=1002-1029, B=1032-1037
9J1PEM2.99 ÅA=848-894, A=909-1037
8ZH8EM3.19 ÅA=848-989, A=991-1000, A=1002-1029, A=1032-1037
8JHIEM3.2 ÅA=655-707, A=847-1037
8GY7EM3.3 ÅA=671-675, A=677-710, A=848-894, A=909-1037
8JHBEM3.3 ÅA=655-707, A=847-896, A=907-1037

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