P04972: Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit… (PDE6G)

Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit… (PDE6G) is a 87-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04972.

Gene
PDE6G
Organism
Bos taurus
Length
87 residues
Mean pLDDT
66.4
Model
AF-P04972-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 66.4 (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 accurate0%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution69%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Inhibitory gamma subunit of the rod-specific cGMP phosphodiesterase (PDE6) complex, which hydrolyzes 3',5'-cyclic GMP in the phototransduction cascade. The PDE6 holoenzyme consists of two catalytic subunits (PDE6A and PDE6B) and two inhibitory gamma subunits (PubMed:33007200, PubMed:38159849). Light-activated GNAT1 relieves gamma subunit-mediated inhibition, enabling the catalytic subunits to hydrolyze cGMP and thereby mediate visual signal transduction and amplification (PubMed:33007200, PubMed:38159849)

Subunit structure

Tetramer composed of two catalytic chains (alpha and beta) and two inhibitory chains (gamma) (PubMed:33007200, PubMed:38159849). Interacts with GNAT1; two GNAT1-GTP molecules bind both the catalytic core (PDE6A and PDE6B) and the inhibitory PDE6G subunits, inducing conformational rearrangements that relieve inhibition and activate catalysis (PubMed:33007200, PubMed:38159849)

Subcellular location

Cell projection, cilium, photoreceptor outer segment

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1FQJX-ray2.02 ÅC=46-87
8UGBEM3.0 ÅC/D=1-87
9CXIEM3.0 ÅC/D=1-87
10OZEM3.06 ÅC/D=1-87
8UFIEM3.1 ÅC/D=1-87
9CXHEM3.1 ÅC/D=1-87
9CXJEM3.1 ÅC/D=1-87
7JSNEM3.2 ÅC/D=1-87
8UGSEM3.2 ÅC/D=1-87
8ULGEM3.2 ÅC/D=1-87
6MZBEM3.4 ÅC/D=1-87
3JABEM11.0 ÅD/P=70-87
3JBQEM11.0 ÅD/X=70-87
2JU4NMRA=1-87

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