P13637: Sodium/potassium-transporting ATPase subunit alpha-3 (ATP1A3)

Sodium/potassium-transporting ATPase subunit alpha-3 (ATP1A3) is a 1013-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13637.

Gene
ATP1A3
Organism
Homo sapiens
Length
1013 residues
Mean pLDDT
88.8
Model
AF-P13637-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.8 (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 accurate62%
70 to 90Confident: backbone generally right34%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Neuron-specific alpha catalytic component of the Na(+)/K(+)-transporting ATPase, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane (PubMed:36075933). Transports 3 Na(+) ions out of the cell and 2 K(+) ions into the cell for each ATP hydrolyze against their electrochemical gradients to maintain ion concentration gradients across the membranes (By similarity). In the brain, ATP1A3 is critical for neuronal cell signaling and for maintenance of electrochemical stability, enabling cell excitation and action potential propagation (PubMed:33880529, PubMed:36075933)

Subunit structure

The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit, called FXYD. There are four, three and seven isoforms for the alpha, beta and regulatory subunits, respectively, among which the expression of the alpha isoforms is tissue-specific. Interacts with regulatory subunit FXYD1 (By…

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
8D3VEM3.4 ÅA=1-1013
8D3WEM3.5 ÅA=1-1013
8D3UEM3.7 ÅA=18-1013
8D3YEM3.9 ÅA=1-1013
8D3XEM4.1 ÅA=1-1013

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