P13738: Na(+)/H(+) antiporter NhaA (nhaA)

Na(+)/H(+) antiporter NhaA (nhaA) is a 388-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13738.

Gene
nhaA
Organism
Escherichia coli (strain K12)
Length
388 residues
Mean pLDDT
89.3
Model
AF-P13738-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.3 (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 accurate64%
70 to 90Confident: backbone generally right31%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons (PubMed:1645730, PubMed:23836890, PubMed:2839489, PubMed:7737413, PubMed:8019504, PubMed:8383669). Plays an important role in the regulation of intracellular pH, cellular Na(+) content and cell volume (PubMed:33129932). Catalyzes the exchange of 2 H(+) per Na(+) (PubMed:23836890, PubMed:8383669). This stoichiometry applies at both neutral and alkaline pH values (PubMed:8383669). In addition, can also transport lithium and is involved in lithium detoxification (PubMed:22915592, PubMed:27021484, PubMed:7737413, PubMed:8019504). Binding of the Li(+) and H(+) ligands to NhaA is coupled and antagonistic (PubMed:27021484)

Subunit structure

Monomer (PubMed:17635927). Homodimer (PubMed:11258962, PubMed:15988517, PubMed:17635927, PubMed:19396973, PubMed:25422503). Under routine stress conditions, the monomeric form is fully functional (PubMed:17635927, PubMed:23836890). However, the dimeric form is much more efficient in conferring growth resistance under extreme stress conditions (PubMed:17635927)

Subcellular location

Cell inner membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7S24X-ray2.2 ÅA=1-388
8PS0EM3.37 ÅA/B=1-388
1ZCDX-ray3.45 ÅA/B=1-388
4ATVX-ray3.5 ÅA/B/C/D=1-388
4AU5X-ray3.7 ÅA/B/C/D=1-388
3FI1EM7.0 ÅA=9-384

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