Q96DB9: FXYD domain-containing ion transport regulator 5 (FXYD5)

FXYD domain-containing ion transport regulator 5 (FXYD5) is a 178-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96DB9.

Gene
FXYD5
Organism
Homo sapiens
Length
178 residues
Mean pLDDT
58.4
Model
AF-Q96DB9-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 58.4 (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 accurate9%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution32%
Below 50Very low: often disordered regions43%

What pLDDT means and how to read it

Function

Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane (By similarity). May increase NKA activity by increasing the apparent affinity for Na(+) (PubMed:18263667). Involved in down-regulation of E-cadherin which results in reduced cell adhesion. Promotes metastasis (PubMed:11756660)

Subunit structure

Regulatory subunit of the sodium/potassium-transporting ATPase which is composed of a catalytic alpha subunit, a non-catalytic beta subunit and an additional regulatory subunit. The regulatory subunit, a member of the FXYD protein family, modulates the enzymatic activity in a tissue- and isoform-specific way by changing affinities of the Na+/K+-ATPase toward Na(+), K(+) or ATP

Subcellular location

Cell membrane, Basolateral cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9KCIEM2.9 ÅC=1-178
9KCGEM3.1 ÅC=1-178
9KCJEM3.1 ÅC=1-178

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