Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (NHERF1) is a 358-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14745.
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The mean pLDDT of this model is 72.8 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 10% |
| 70 to 90 | Confident: backbone generally right | 55% |
| 50 to 70 | Low: treat with caution | 22% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules. Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate…
Homodimer, and heterodimer with NHERF2. Binds the N-termini of EZR, RDX and MSN. Binds the C-termini of PDGFRA, PDGFRB, ADRB2, NOS2 and CFTR. Binds ARHGAP17, EPI64, RACK1, OPRK1, GNAQ, CTNNB1 and PLCB3. Binds PDZK1 (By similarity). Interacts with CLCN3. Binds the C-terminus of PAG1. In resting T-cells, part of a PAG1-NHERF1-MSN complex which is disrupted upon TCR activation. Forms a complex with…
Cytoplasm, Apical cell membrane, Endomembrane system, Cell projection, filopodium, Cell projection, ruffle, Cell projection, microvillus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4N6X | X-ray | 1.05 Å | A=11-99 |
| 4LMM | X-ray | 1.1 Å | A=11-99 |
| 4MPA | X-ray | 1.1 Å | A=11-99 |
| 4JL7 | X-ray | 1.16 Å | A=11-95 |
| 9RXT | X-ray | 1.36 Å | A=11-99 |
| 9RXQ | X-ray | 1.38 Å | A/B=11-99 |
| 4Q3H | X-ray | 1.44 Å | A/B=150-235 |
| 4PQW | X-ray | 1.47 Å | A=11-94 |
| 1G9O | X-ray | 1.5 Å | A=11-99 |
| 2OZF | X-ray | 1.5 Å | A=150-235 |
| 1I92 | X-ray | 1.7 Å | A=11-99 |
| 1GQ4 | X-ray | 1.9 Å | A=11-94 |
| 1GQ5 | X-ray | 2.2 Å | A=11-96 |
| 6RQR | X-ray | 2.2 Å | A/B=150-269 |
| 2D10 | X-ray | 2.5 Å | E/F/G/H=331-358 |
| 1SGH | X-ray | 3.5 Å | B=321-358 |
| 2JXO | NMR | A=150-240 | |
| 2KJD | NMR | A=150-270 | |
| 2KRG | NMR | A=150-358 | |
| 2M0T | NMR | A=11-120 |
Showing 20 of 22 experimental structures (best resolution first).
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