P48357: Leptin receptor (LEPR)

Leptin receptor (LEPR) is a 1165-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P48357.

Gene
LEPR
Organism
Homo sapiens
Length
1165 residues
Mean pLDDT
66.0
Model
AF-P48357-F1 v6
Model created
1 Aug 2025
PDB structures
9

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 66.0 (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 accurate21%
70 to 90Confident: backbone generally right37%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions33%

What pLDDT means and how to read it

Function

Receptor for hormone LEP/leptin (Probable) (PubMed:22405007). On ligand binding, mediates LEP central and peripheral effects through the activation of different signaling pathways such as JAK2/STAT3 and MAPK cascade/FOS. In the hypothalamus, LEP acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones (By similarity) (PubMed:9537324). In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is…

Subunit structure

Present as a mixture of monomers and dimers (Probable). The phosphorylated receptor binds a number of SH2 domain-containing proteins such as JAK2, STAT3, PTPN11, and SOCS3 (By similarity) (PubMed:9600917). Interaction with SOCS3 inhibits JAK/STAT signaling and MAPK cascade (By similarity)

Subcellular location

Cell membrane, Basolateral 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
3V6OX-ray1.95 ÅA/B=428-633
6E2PX-ray2.83 ÅC/D=863-933
8X85EM3.58 ÅA/B=21-839
7Z3QX-ray3.62 ÅB/D/F=428-635
8X81EM3.77 ÅA/B/C=21-839
8X80EM3.88 ÅA/B/C=21-839
8AVEEM5.62 ÅB/D=22-839
8AVFEM6.45 ÅB/D/F=22-839
8AVOEM6.84 ÅB/D/F=22-839

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.