Q8VHW5: Voltage-dependent calcium channel gamma-8 subunit (Cacng8)

Voltage-dependent calcium channel gamma-8 subunit (Cacng8) is a 421-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8VHW5.

Gene
Cacng8
Organism
Rattus norvegicus
Length
421 residues
Mean pLDDT
58.8
Model
AF-Q8VHW5-F1 v6
Model created
1 Aug 2025
PDB structures
12

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Model confidence (pLDDT)

The mean pLDDT of this model is 58.8 (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 accurate13%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions49%

What pLDDT means and how to read it

Function

Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit (By similarity). Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state

Subunit structure

Interacts with CACNA1C. Identified in a complex with the L-type calcium channel subunits CACNA1C, CACNA2D1 and either CACNB1 or CACNB2 (By similarity). Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5 and CACNG7. Interacts with CNIH2 (By similarity). Found in a complex…

Subcellular location

Cell membrane, Postsynaptic density membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8AYNEM2.8 ÅI/J=2-417
7OCEEM3.1 ÅI/J=2-417
8AYLEM3.2 ÅI/J=2-417
8AYMEM3.3 ÅI/J=2-417
8AYOEM3.3 ÅI/J=2-417
7OCAEM3.4 ÅI/J=2-417
7OCDEM3.5 ÅI/J=2-417
7QHBEM3.5 ÅI/J=2-417
7OCFEM3.6 ÅI/J=2-417
7QHHEM3.6 ÅI/J=2-417
6QKCEM4.1 ÅI/J=2-417
6QKZEM6.3 ÅI/J=2-417

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