P18545: 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 Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P18545.

Gene
PDE6G
Organism
Homo sapiens
Length
87 residues
Mean pLDDT
67.3
Model
AF-P18545-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 67.3 (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 right33%
50 to 70Low: treat with caution67%
Below 50Very low: often disordered regions0%

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. Light-activated GNAT1 relieves gamma subunit-mediated inhibition, enabling the catalytic subunits to hydrolyze cGMP and thereby mediate visual signal transduction and amplification

Subunit structure

Tetramer composed of two catalytic chains (alpha and beta) and two inhibitory chains (gamma). 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

Subcellular location

Cell projection, cilium, photoreceptor outer segment

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3JWRX-ray2.99 ÅC/D=70-87

More AlphaFold highlights

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