P25090: N-formyl peptide receptor 2 (FPR2)

N-formyl peptide receptor 2 (FPR2) is a 351-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P25090.

Gene
FPR2
Organism
Homo sapiens
Length
351 residues
Mean pLDDT
84.8
Model
AF-P25090-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.8 (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 accurate66%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Pattern recognition G protein-coupled receptor (GPCR) that recognizes peptides with N-terminal formyl methionine, which are derived from invading pathogens or host mitochondria as pathogen or damage-associated molecular patterns (PAMPs and DAMPs) (PubMed:1374236, PubMed:25605714, PubMed:35217703). Preferentially recognizes longer peptides or peptides with specific sequences such as the phenol-soluble modulin (PSM) family of formylated peptide toxins produced by Staphylococcus aureus (PubMed:30098280). Ligand binding causes a conformation change that triggers signaling via G(i)/GNAI1 inhibiting adenylate cyclase activity, leading to decreased intracellular cAMP levels (PubMed:40080544). In…

Subunit structure

Homodimer; the homodimerization is potentiated in response to the anti-inflammatory agonist ANXA1 and inhibited upon binding of pro-inflammatory agonist serum amyloid A (PubMed:24108355). Heterodimer with FPR1; the heterodimerization with FPR1 is potentiated in response to anti-inflammatory agonists such as lipoxin A4, ANXA1 and Ac2-26 ANXA1 peptide (PubMed:24108355). Forms a complex with…

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8ZBWEM2.58 ÅR=19-317
6LW5X-ray2.8 ÅA=3-322
7WVXEM2.8 ÅR=2-347
7T6UEM2.9 ÅR=1-342
7WVVEM2.9 ÅR=2-347
7T6SEM3.0 ÅR=1-342
7WVYEM3.0 ÅR=2-347
7T6VEM3.1 ÅR=1-342
7WVWEM3.1 ÅR=2-347
6OMMEM3.17 ÅR=1-342
8Y62EM3.2 ÅR=1-351
8Y63EM3.2 ÅR=1-351
9JHJEM3.2 ÅR=1-351

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