P51577: P2X purinoceptor 4 (P2rx4)

P2X purinoceptor 4 (P2rx4) is a 388-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P51577.

Gene
P2rx4
Organism
Rattus norvegicus
Length
388 residues
Mean pLDDT
89.3
Model
AF-P51577-F1 v6
Model created
1 Aug 2025
PDB structures
2

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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 accurate66%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

ATP-gated nonselective transmembrane cation channel permeable to potassium, sodium and calcium. CTP, but not GTP or UTP, functions as a weak affinity agonist for P2RX4 (PubMed:28332633, PubMed:8622997). Activated by extracellularly released ATP, it plays multiple role in immunity and central nervous system physiology (PubMed:15985462, PubMed:24762105). Plays a key role in initial steps of T-cell activation and Ca(2+) microdomain formation (By similarity). Also participates in basal T-cell activity without TCR/CD3 stimulation (By similarity). Promotes the differentiation and activation of Th17 cells via expression of retinoic acid-related orphan receptor C/RORC (By similarity). Upon…

Subunit structure

Functional P2RXs are organized as homomeric and heteromeric trimers. Forms heterotrimer with P2RX1 (PubMed:15686495). Interacts with P2RX7 (via C-terminus); this interaction is functional only in the presence of ATP (By similarity). Forms heterotrimer with P2RX4; functional differences between homomeric P2RX4 and P2RX4/6 heterotrimer are minor (PubMed:12077178). Interacts with AP1M2…

Subcellular location

Cell membrane, Lysosome membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2BP5X-ray2.8 ÅP=375-384
2RUPNMRA=111-167

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