P09471: Guanine nucleotide-binding protein G(o) subunit alpha (GNAO1)

Guanine nucleotide-binding protein G(o) subunit alpha (GNAO1) is a 354-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P09471.

Gene
GNAO1
Organism
Homo sapiens
Length
354 residues
Mean pLDDT
94.5
Model
AF-P09471-F1 v6
Model created
1 Aug 2025
PDB structures
83

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Model confidence (pLDDT)

The mean pLDDT of this model is 94.5 (very high 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 accurate87%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades, such as regulation of postsynaptic neurotransmitter release (PubMed:29925951, PubMed:33408414, PubMed:39103320). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:39103320). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:39103320). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (By similarity). Both GDP release and GTP hydrolysis are modulated by…

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma (PubMed:29925951, PubMed:39103320, PubMed:34685729). The alpha chain contains the guanine nucleotide binding site (PubMed:29925951, PubMed:39103320). Forms a complex with GNB1 and GNG3 (PubMed:34685729). Forms a complex with GNB1 and GNG2; this complex associates with Mu-type opioid receptor OPRM1, D(2) dopamine receptor DRD2, neurotensin…

Subcellular location

Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9BSBEM2.32 ÅA=1-354
9VJEEM2.47 ÅB=1-354
9K20EM2.65 ÅB=4-57, B=182-354
9VJ5EM2.69 ÅB=1-354
8E9XEM2.7 ÅB=4-354
9PLOEM2.74 ÅA=1-354
9VNFEM2.74 ÅB=1-354
8YN7EM2.77 ÅA=4-354
8YN8EM2.77 ÅA=4-354
9KVPEM2.79 ÅA=4-57, A=182-354
7W2ZEM2.8 ÅA=182-354
8XXHEM2.8 ÅA=4-57, A=182-354
8DZQEM2.82 ÅB=1-354
9VMYEM2.86 ÅB=1-354
8FN1EM2.88 ÅB=1-57, B=182-354
8I95EM2.88 ÅA=4-57, A=182-354
9KV6EM2.88 ÅA=4-57, A=182-354
6K41EM2.9 ÅA=1-354
7D77EM2.9 ÅA=4-354
9DYEEM2.9 ÅA=1-354

Showing 20 of 83 experimental structures (best resolution first).

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