P30988: Calcitonin receptor (CALCR)

Calcitonin receptor (CALCR) is a 474-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P30988.

Gene
CALCR
Organism
Homo sapiens
Length
474 residues
Mean pLDDT
78.7
Model
AF-P30988-F1 v6
Model created
1 Aug 2025
PDB structures
30

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.7 (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 accurate43%
70 to 90Confident: backbone generally right32%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

G protein-coupled receptor activated by ligand peptides amylin (IAPP), calcitonin (CT/CALCA) and calcitonin gene-related peptide type 1 (CGRP1/CALCA) (PubMed:35324283, PubMed:38603770). CALCR interacts with receptor-activity-modifying proteins RAMP1, 2 and 3 to form receptor complexes AMYR1, 2 and 3, respectively (PubMed:35324283, PubMed:38603770). IAPP, CT and CGRP1 activate CALCR and AMYRs with distinct modes of receptor activation resulting in specific phenotypes (PubMed:35324283, PubMed:38603770). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors. Activates…

Subunit structure

Heterodimer of CALCR and RAMP1, RAMP2 or RAMP3; the receptor complexes function as AMYR1, AMYR2 and AMYR3 receptors, respectively, and respond to amylin/IAPP, calcitonin/CT and CGRP1 ligands (PubMed:35324283, PubMed:38603770). Interacts with GPRASP2 (PubMed:15086532)

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6PFOX-ray1.78 ÅA/B=38-141
8F0KEM1.9 ÅR=25-474
8F0JEM2.0 ÅR=25-474
8F2BEM2.0 ÅR=25-474
5II0X-ray2.1 ÅA/B/C=25-144
7TYFEM2.2 ÅR=25-474
8F2AEM2.2 ÅR=25-474
9BP3EM2.2 ÅR=25-474
9BUBEM2.3 ÅR=25-474
7TZFEM2.4 ÅR=25-474
9AUCEM2.4 ÅR=25-474
9BUDEM2.5 ÅR=25-474
7TYXEM2.55 ÅR=25-474
7TYNEM2.6 ÅR=25-474
7TYOEM2.7 ÅR=25-474
9BQ3EM2.8 ÅR=25-474
6PGQX-ray2.85 ÅA=39-141
7TYWEM3.0 ÅR=25-474
7TYYEM3.0 ÅR=25-474
9BTWEM3.0 ÅR=25-474

Showing 20 of 30 experimental structures (best resolution first).

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