P21728: D(1A) dopamine receptor (DRD1)

D(1A) dopamine receptor (DRD1) is a 446-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P21728.

Gene
DRD1
Organism
Homo sapiens
Length
446 residues
Mean pLDDT
72.4
Model
AF-P21728-F1 v6
Model created
1 Aug 2025
PDB structures
31

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.4 (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 accurate41%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions27%

What pLDDT means and how to read it

Function

G protein-coupled receptor for dopamine, a catecholamine neurotransmitter hormone that functions as the brain's 'reward chemical', driving motivation, reinforcement learning and pleasure (PubMed:11500503, PubMed:33571431, PubMed:33571432, PubMed:33750903, PubMed:34083522, PubMed:35676276, PubMed:35687690, PubMed:37221270). Dopamine 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:33571431, PubMed:33571432, PubMed:33750903, PubMed:34083522, PubMed:35676276, PubMed:35687690). Dopamine receptors can be classified in two categories: (1) DRD1…

Subunit structure

Interacts with DNAJC14 via its C-terminus (By similarity). Interacts with DORIP1 (By similarity). Interacts with DRD2 (By similarity). Interacts with DRD3 (By similarity). Interacts with GHSR; forms a heteromer with GHSR in hippocampal neurons (By similarity)

Subcellular location

Postsynaptic cell membrane, Cell projection, dendritic spine membrane, Cell projection, cilium membrane, Endoplasmic reticulum membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9LLJEM2.61 ÅR=2-446
9LLFEM2.64 ÅR=2-446
9I54EM2.72 ÅR=1-446
9LLHEM2.73 ÅR=2-446
9LLGEM2.77 ÅR=2-220, R=235-270, R=276-446
9I52EM2.8 ÅR=1-446
7JVPEM2.9 ÅR=1-446
9LLEEM2.9 ÅR=2-446
9LWCEM2.9 ÅR=1-446
7JV5EM3.0 ÅR=1-446
7JVQEM3.0 ÅR=1-446
7LJCEM3.0 ÅR=1-446
7X2FEM3.0 ÅF=1-446
8JXSEM3.0 ÅA=11-362
9LLIEM3.0 ÅR=2-220, R=276-446
7CKZEM3.1 ÅR=1-446
7F0TEM3.1 ÅF=1-446
7F1OEM3.13 ÅF=1-446
7CKYEM3.2 ÅR=1-446
7LJDEM3.2 ÅR=1-446

Showing 20 of 31 experimental structures (best resolution first).

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