P19634: Sodium/hydrogen exchanger 1 (SLC9A1)

Sodium/hydrogen exchanger 1 (SLC9A1) is a 815-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19634.

Gene
SLC9A1
Organism
Homo sapiens
Length
815 residues
Mean pLDDT
67.6
Model
AF-P19634-F1 v6
Model created
1 Aug 2025
PDB structures
20

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Model confidence (pLDDT)

The mean pLDDT of this model is 67.6 (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 right37%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions29%

What pLDDT means and how to read it

Function

Electroneutral Na(+) /H(+) antiporter that extrudes Na(+) in exchange for external protons driven by the inward sodium ion chemical gradient, protecting cells from acidification that occurs from metabolism (PubMed:11350981, PubMed:11532004, PubMed:14680478, PubMed:15035633, PubMed:15677483, PubMed:17073455, PubMed:17493937, PubMed:22020933, PubMed:27650500, PubMed:32130622, PubMed:7110335, PubMed:7603840). Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry (By similarity). Plays a key role in maintening intracellular pH neutral and cell volume, and thus is important for cell growth, proliferation, migration and survival (PubMed:12947095, PubMed:15096511,…

Subunit structure

Homodimer; dimerization is crucial for its function (PubMed:15323573, PubMed:17073455, PubMed:34108458). Oligomer (By similarity). Interacts with CALM1 in a calcium-dependent manner (PubMed:12809501, PubMed:18757828, PubMed:30287853). Interacts with TESC (PubMed:11696366, PubMed:12809501, PubMed:30287853). Interacts (via the C-terminal domain) with CHP1; the interaction occurs at the plasma…

Subcellular location

Cell membrane, Basolateral cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6NUCX-ray1.9 ÅC=679-723
6NUFX-ray1.9 ÅC=679-723
9NXEX-ray2.09 ÅC=679-723
2YGGX-ray2.23 ÅA=622-689
6NUUX-ray2.3 ÅC=679-723
2BECX-ray2.7 ÅB=503-545
23XKEM3.1 ÅA/B=1-815
23XOEM3.16 ÅA/B=1-815
23XMEM3.24 ÅA/B=1-815
7DSWEM3.3 ÅA/B=87-506
7DSVEM3.4 ÅA/B=87-558
7DSXEM3.5 ÅA/B=85-593
1Y4ENMRA=155-180
2E30NMRB=503-545
2HTGNMRA=250-274
2KBVNMRA=447-472
2L0ENMRA=226-250
2MDFNMRA=226-274
6BJFNMRA=431-443
6ZBINMRB/C=622-657

More AlphaFold highlights

About this viewer

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