O60896: Receptor activity-modifying protein 3 (RAMP3)

Receptor activity-modifying protein 3 (RAMP3) is a 148-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60896.

Gene
RAMP3
Organism
Homo sapiens
Length
148 residues
Mean pLDDT
87.6
Model
AF-O60896-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.6 (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 accurate74%
70 to 90Confident: backbone generally right7%
50 to 70Low: treat with caution16%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Accessory protein that interacts with and modulates the function of G protein-coupled receptors including calcitonin gene-related peptide type 1 receptor (CALCRL), calcitonin receptor (CALCR) and G protein-coupled estrogen receptor 1 (GPER1) (PubMed:23674134, PubMed:9620797). Required for the transport of CALCRL and GPER1 receptors to the plasma membrane (PubMed:23674134, PubMed:9620797). Plays a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a GPER1-dependent manner (PubMed:23674134). Together with CALCRL, form a receptor complex for adrenomedullin/ADM and intermedin/ADM2 (PubMed:32296767). Together with CALCR, act as a receptor complex for…

Subunit structure

Heterodimer of CALCRL and RAMP3; interaction induces allosteric modulation of CALCRL function and ligand specificity for adrenomedullin/ADM and intermedin/ADM2 (PubMed:32296767). Heterodimer of CALCR and RAMP3; interaction form the receptor complex AMYR3 for amylin/IAPP (PubMed:35324283). Interacts with GPER1 (PubMed:23674134)

Subcellular location

Cell membrane, Membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8F0KEM1.9 ÅE=24-148
8F2BEM2.0 ÅE=24-148
8F2AEM2.2 ÅE=24-148
6UVAEM2.3 ÅE=24-148
6UUSEM2.4 ÅE=24-148
7TZFEM2.4 ÅE=24-148
9BTWEM3.0 ÅE=24-148

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