P63212: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (GNG2)

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (GNG2) is a 71-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63212.

Gene
GNG2
Organism
Bos taurus
Length
71 residues
Mean pLDDT
89.4
Model
AF-P63212-F1 v6
Model created
1 Aug 2025
PDB structures
214

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.4 (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 accurate72%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems (By similarity). The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (By similarity). Involved in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction (By similarity)

Subunit structure

G proteins are composed of 3 units, alpha, beta and gamma (PubMed:8521505). In this context, interacts with GNB2 (By similarity). The heterodimer formed by GNB1 and GNG2 interacts with ARHGEF5 (By similarity). The heterodimer formed by GNB1 and GNG2 interacts with GRK2 (PubMed:12764189). The heterodimer formed by GNB1 and GNG2 interacts with the ghrelin receptor GHSR (By similarity). Forms a…

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3V5WX-ray2.07 ÅG=1-71
1GP2X-ray2.3 ÅG=1-71
5WG4X-ray2.31 ÅG=1-71
9IJEEM2.34 ÅC=10-61
1GG2X-ray2.4 ÅG=1-71
4MK0X-ray2.4 ÅG=6-64
8YK0EM2.4 ÅG=7-63
8Z9OEM2.4 ÅG=6-62
22ESEM2.43 ÅC=1-71
6U7CX-ray2.44 ÅG=1-71
8JISEM2.46 ÅG=6-62
9M0REM2.47 ÅG=1-71
3PVUX-ray2.48 ÅG=1-68
8Y01EM2.48 ÅG=1-71
8YKVEM2.48 ÅG=1-71
3PVWX-ray2.49 ÅG=1-68
9M1OEM2.49 ÅG=1-71
1OMWX-ray2.5 ÅG=1-68
7DUQEM2.5 ÅG=2-71
7EVMEM2.5 ÅG=2-71

Showing 20 of 214 experimental structures (best resolution first).

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