5-hydroxytryptamine receptor 2A (HTR2A) is a 471-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P28223.
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The mean pLDDT of this model is 73.8 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 51% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 27% |
What pLDDT means and how to read it
G protein-coupled receptor for 5-hydroxytryptamine (serotonin) (PubMed:1330647, PubMed:18703043, PubMed:19057895, PubMed:21645528, PubMed:22300836, PubMed:35084960, PubMed:38552625). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD) (PubMed:28129538, PubMed:35084960). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors (PubMed:28129538, PubMed:35084960). HTR2A is coupled to G(q)/G(11) G alpha proteins and activates…
Interacts (via C-terminus) with MPDZ and PATJ (PubMed:11150294, PubMed:14988405). May interact (via C-terminus) with MPP3, PRDX6, DLG4, DLG1, CASK, APBA1 and MAGI2 (PubMed:14988405). Interacts with GRM2 and DRD2; this may affect signaling (PubMed:18297054, PubMed:21645528, PubMed:22300836)
Cell membrane, Cell projection, dendrite, Cell projection, axon, Cytoplasmic vesicle, Membrane, caveola, Presynapse
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7WC8 | X-ray | 2.45 Å | A=67-265, A=312-403 |
| 7WC9 | X-ray | 2.5 Å | A=67-265, A=312-403 |
| 9AS8 | EM | 2.54 Å | A=1-471 |
| 7WC6 | X-ray | 2.6 Å | A=67-265, A=312-403 |
| 7WC7 | X-ray | 2.6 Å | A=67-265, A=312-403 |
| 9LL8 | EM | 2.62 Å | R=1-471 |
| 8JT8 | X-ray | 2.7 Å | A=70-265, A=313-403 |
| 9AS7 | EM | 2.72 Å | A=1-471 |
| 9LL9 | EM | 2.76 Å | R=1-471 |
| 8UWL | EM | 2.8 Å | A=66-404 |
| 9J87 | EM | 2.84 Å | A=66-404 |
| 9LL7 | EM | 2.84 Å | R=1-471 |
| 6A94 | X-ray | 2.9 Å | A/B=70-265, A/B=313-403 |
| 7VOE | X-ray | 2.9 Å | A=70-265, A=313-403 |
| 9LLB | EM | 2.98 Å | R=1-471 |
| 6A93 | X-ray | 3.0 Å | A/B=70-265, A/B=313-403 |
| 8V6U | EM | 3.0 Å | A=66-404 |
| 9AS4 | EM | 3.06 Å | A=1-471 |
| 9AS6 | EM | 3.07 Å | A=1-471 |
| 9UJM | EM | 3.07 Å | C=66-405 |
Showing 20 of 39 experimental structures (best resolution first).
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