P42702: Leukemia inhibitory factor receptor (LIFR)

Leukemia inhibitory factor receptor (LIFR) is a 1097-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P42702.

Gene
LIFR
Organism
Homo sapiens
Length
1097 residues
Mean pLDDT
73.8
Model
AF-P42702-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.8 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate38%
70 to 90Confident: backbone generally right31%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions25%

What pLDDT means and how to read it

Function

Functions as a membrane-bound signal-transducing subunit either in complex with IL6ST/gp130 or as part of the ciliary neurotrophic factor receptor (CNTFR) complex composed by CNTFR, IL6ST/gp130 and LIFR (PubMed:11285233, PubMed:11294841, PubMed:1542794, PubMed:39532904, PubMed:9030543, PubMed:9188471). Signal transmission is initiated either by binding directly to cytokines, such as OSM or LIF or CTF1, or through the binding of other cytokines, like CNTF, CLCF1 or the heterodimeric complex CRLF1-CLCF1 to the non-signaling receptor CNTFR; ligand binding induces heterodimerization of IL6ST/gp130 and LIFR which activates JAK tyrosine kinases bound to their intracellular domains…

Subunit structure

Heterodimer composed of LIFR and IL6ST (PubMed:1542794). Component of the ciliary neurotrophic factor receptor (CNTFR) complex composed of CNTFR, LIFR and IL6ST; CNTF binding to CNTFR induces heterodimerization of LIFR and IL6ST (PubMed:18775332, PubMed:36930708)

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
8D74EM3.03 ÅB=45-833
3E0GX-ray3.1 ÅA=52-534
8D6AEM3.54 ÅB=45-833
8V2AEM3.59 ÅC=45-833
8D7REM3.9 ÅB=45-833
8V29EM3.99 ÅC=45-833

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