P21730: C5a anaphylatoxin chemotactic receptor 1 (C5AR1)

C5a anaphylatoxin chemotactic receptor 1 (C5AR1) is a 350-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P21730.

Gene
C5AR1
Organism
Homo sapiens
Length
350 residues
Mean pLDDT
85.8
Model
AF-P21730-F1 v6
Model created
1 Aug 2025
PDB structures
19

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.8 (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 accurate67%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a, stimulating chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production (PubMed:10636859, PubMed:15153520, PubMed:1847994, PubMed:29300009, PubMed:36806352, PubMed:7622471, PubMed:8182049, PubMed:9553099). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:36806352, PubMed:37852260). C5AR1 is coupled to G(i)/G(o) (GNAI1 or GNAO1) G alpha proteins and mediates inhibition of adenylate cyclase (PubMed:36806352, PubMed:37852260).…

Subunit structure

Homodimer (PubMed:29300009). May also form higher-order oligomers (PubMed:12835319). Interacts (when phosphorylated) with ARRB1 and ARRB2; the interaction is associated with internalization of the receptor and short-term desensitization to the ligand (PubMed:12464600, PubMed:37209686)

Subcellular location

Cell membrane, Cytoplasmic vesicle

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6C1RX-ray2.2 ÅB=30-331
5O9HX-ray2.7 ÅA/B=31-333
7Y67EM2.8 ÅD=1-330
6C1QX-ray2.9 ÅB=30-331
7Y64EM2.9 ÅD=1-330
7Y66EM2.9 ÅD=1-330
8HK5EM3.0 ÅA=1-350
9KUGEM3.07 ÅA=2-350
9UMREM3.15 ÅD=2-350
7Y65EM3.2 ÅD=1-330
9UMXEM3.2 ÅA=2-350
8IA2EM3.21 ÅA=2-350
8I0NEM3.26 ÅU/V=334-342
8JZZEM3.31 ÅA=2-350
8GO8EM3.41 ÅU/V=331-350
8JZPEM3.45 ÅA=2-350
8I0ZEM4.33 ÅG/U/V=331-350
8GOOEM4.4 ÅG/U/V=331-350
2K3UNMRB=7-28

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