Q9NR82: Potassium voltage-gated channel subfamily KQT member 5 (KCNQ5)

Potassium voltage-gated channel subfamily KQT member 5 (KCNQ5) is a 932-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NR82.

Gene
KCNQ5
Organism
Homo sapiens
Length
932 residues
Mean pLDDT
56.4
Model
AF-Q9NR82-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 56.4 (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 accurate20%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions56%

What pLDDT means and how to read it

Function

Pore-forming subunit of the voltage-gated potassium (Kv) channel broadly expressed in brain and involved in the regulation of neuronal excitability (PubMed:10787416, PubMed:10816588, PubMed:11159685, PubMed:28669405). Associates with KCNQ3/Kv7.3 pore-forming subunit to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons (PubMed:10816588, PubMed:11159685). Contributes, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which…

Subunit structure

Homotetramer; forms a functional homotetrameric channel resulting in the expression of a small M-current (PubMed:10816588, PubMed:29429937). Heterotetramer with KCNQ3; forms heterotetrameric M-channel responsible for the native M-current (PubMed:10787416, PubMed:10816588, PubMed:11159685). Heterotetramer with KCNQ1; forms a functional voltage-gated potassium channel (PubMed:24855057). Interacts…

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
9J38EM2.4 ÅA/B/C/D=89-698
6B8QX-ray2.6 ÅA/C/E/G=361-394, A/C/E/G=512-545
9LJ5EM2.9 ÅA/B/D/G=90-698
9LIZEM3.1 ÅA/B/D/G=90-698
9LJ1EM3.2 ÅA/B/D/G=90-698

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