Na(+)/H(+) exchange regulatory cofactor NHE-RF3 (PDZK1) is a 519-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5T2W1.
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The mean pLDDT of this model is 78.1 (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 | 44% |
| 70 to 90 | Confident: backbone generally right | 33% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with NHERF1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. Required for normal cell-surface expression of…
Interacts with PDZK1IP1 and ABCC2. Interacts (via PDZ domains 1 and 3) with SCARB1 (C-terminal domain). Forms a heterodimeric complex with NHERF1. Interacts with AKAP2, BCR, CFTR, SLC22A12, SLC22A4, SLC22A5, NHERF2 and SLC17A1. Component of a complex, composed of PDZK1, SYNGAP1, KLHL17 and NMDA receptors. Interacts (via PDZ1 domain) directly with KLHL17; the interaction is important for…
Membrane, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9RXO | X-ray | 1.2 Å | A/B=132-215 |
| 9RXN | X-ray | 1.36 Å | A/B=6-110 |
| 9RXP | X-ray | 1.43 Å | A/B=375-463 |
| 6EZI | X-ray | 1.5 Å | A=374-460 |
| 9RXR | X-ray | 1.69 Å | A=6-106 |
| 9RXS | X-ray | 2.0 Å | A/B=375-458 |
| 4Q2P | X-ray | 2.05 Å | A/B/C=132-215 |
| 2VSP | X-ray | 2.41 Å | A/B/C/D=375-461 |
| 3TMH | X-ray | 3.8 Å | A/E/I=375-459 |
| 2EEI | NMR | A=132-224 | |
| 2EEJ | NMR | A=376-458 |
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