P19235: Erythropoietin receptor (EPOR)

Erythropoietin receptor (EPOR) is a 508-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19235.

Gene
EPOR
Organism
Homo sapiens
Length
508 residues
Mean pLDDT
66.9
Model
AF-P19235-F1 v6
Model created
1 Aug 2025
PDB structures
22

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Model confidence (pLDDT)

The mean pLDDT of this model is 66.9 (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 accurate34%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions41%

What pLDDT means and how to read it

Function

Receptor for erythropoietin, which mediates erythropoietin-induced erythroblast proliferation and differentiation (PubMed:10388848, PubMed:2163695, PubMed:2163696, PubMed:8662939, PubMed:9774108). Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade (By similarity). In some cell types, can also activate STAT1 and STAT3 (PubMed:11756159). May also activate the LYN tyrosine kinase (By similarity)

Subunit structure

Forms homodimers on EPO stimulation (PubMed:10388848, PubMed:9774108, PubMed:9974392). The tyrosine-phosphorylated form interacts with several SH2 domain-containing proteins including LYN, the adapter protein SH2B2, PTPN6, PTPN11, JAK2, PI3 kinases, STAT5A/B, SOCS3, CRKL (PubMed:12027890, PubMed:7534299). Interacts with INPP5D/SHIP1 (By similarity). SH2B2 binding inhibits the JAK-STAT signaling…

Subcellular location

Cell membrane, Secreted

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1EERX-ray1.9 ÅB/C=26-250
6MOIX-ray2.06 ÅB=32-249
6MOEX-ray2.09 ÅC/D=32-249
8VUIX-ray2.1 ÅD=25-250
1ERNX-ray2.4 ÅA/B=34-246
6MOJX-ray2.43 ÅB=32-249
4Y5VX-ray2.6 ÅC/F/I=32-249
6E2QX-ray2.65 ÅM/N/O/P=273-338
6I4XX-ray2.69 ÅD=422-432
1EBAX-ray2.7 ÅA/B=34-248
1CN4X-ray2.8 ÅA/B=24-249
1EBPX-ray2.8 ÅA/B=34-244
4Y5YX-ray2.85 ÅC/F=32-249
6MOFX-ray2.89 ÅB=32-249
8VVMX-ray2.9 ÅI=25-250
8VVOX-ray3.09 ÅI=25-250
4Y5XX-ray3.15 ÅC/F/I/L=32-249
6MOLX-ray3.16 ÅB/C=32-249
2JIXX-ray3.2 ÅB/C/E=25-249
6MOHX-ray3.2 ÅC/D=32-249

Showing 20 of 22 experimental structures (best resolution first).

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