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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9F33

Cryo-EM structure of Dopamine 3 Receptor:Go complex bound to bitopic FOB02-04A - Conformation A

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005834cellular_componentheterotrimeric G-protein complex
A0005886cellular_componentplasma membrane
A0006904biological_processvesicle docking involved in exocytosis
A0006936biological_processmuscle contraction
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0007198biological_processadenylate cyclase-inhibiting serotonin receptor signaling pathway
A0007212biological_processG protein-coupled dopamine receptor signaling pathway
A0007626biological_processlocomotory behavior
A0008016biological_processregulation of heart contraction
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019001molecular_functionguanyl nucleotide binding
A0030425cellular_componentdendrite
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031821molecular_functionG protein-coupled serotonin receptor binding
A0031852molecular_functionmu-type opioid receptor binding
A0042734cellular_componentpresynaptic membrane
A0044297cellular_componentcell body
A0045211cellular_componentpostsynaptic membrane
A0046676biological_processnegative regulation of insulin secretion
A0046872molecular_functionmetal ion binding
A0051430molecular_functioncorticotropin-releasing hormone receptor 1 binding
A0098688cellular_componentparallel fiber to Purkinje cell synapse
A0098978cellular_componentglutamatergic synapse
A0098982cellular_componentGABA-ergic synapse
A0099170biological_processpostsynaptic modulation of chemical synaptic transmission
B0001750cellular_componentphotoreceptor outer segment
B0001917cellular_componentphotoreceptor inner segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007204biological_processpositive regulation of cytosolic calcium ion concentration
B0008283biological_processcell population proliferation
B0010659biological_processcardiac muscle cell apoptotic process
B0030159molecular_functionsignaling receptor complex adaptor activity
B0030425cellular_componentdendrite
B0030507molecular_functionspectrin binding
B0042622cellular_componentphotoreceptor outer segment membrane
B0044297cellular_componentcell body
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0071456biological_processcellular response to hypoxia
C0005515molecular_functionprotein binding
C0005834cellular_componentheterotrimeric G-protein complex
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
C0016020cellular_componentmembrane
C0031681molecular_functionG-protein beta-subunit binding
C0045202cellular_componentsynapse
C0048144biological_processfibroblast proliferation
C0070062cellular_componentextracellular exosome
C0071380biological_processcellular response to prostaglandin E stimulus
C0071870biological_processcellular response to catecholamine stimulus
R0001591molecular_functiondopamine neurotransmitter receptor activity, coupled via Gi/Go
R0001963biological_processsynaptic transmission, dopaminergic
R0002031biological_processG protein-coupled receptor internalization
R0004930molecular_functionG protein-coupled receptor activity
R0005515molecular_functionprotein binding
R0005886cellular_componentplasma membrane
R0006091biological_processgeneration of precursor metabolites and energy
R0006874biological_processintracellular calcium ion homeostasis
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
R0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
R0007195biological_processadenylate cyclase-inhibiting dopamine receptor signaling pathway
R0007611biological_processlearning or memory
R0007612biological_processlearning
R0007626biological_processlocomotory behavior
R0008218biological_processbioluminescence
R0008542biological_processvisual learning
R0009410biological_processresponse to xenobiotic stimulus
R0014059biological_processregulation of dopamine secretion
R0016020cellular_componentmembrane
R0032467biological_processpositive regulation of cytokinesis
R0032922biological_processcircadian regulation of gene expression
R0034776biological_processresponse to histamine
R0035176biological_processsocial behavior
R0042220biological_processresponse to cocaine
R0042417biological_processdopamine metabolic process
R0043266biological_processregulation of potassium ion transport
R0043278biological_processresponse to morphine
R0045202cellular_componentsynapse
R0045471biological_processresponse to ethanol
R0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
R0045776biological_processnegative regulation of blood pressure
R0045840biological_processpositive regulation of mitotic nuclear division
R0046717biological_processacid secretion
R0048148biological_processbehavioral response to cocaine
R0048715biological_processnegative regulation of oligodendrocyte differentiation
R0050482biological_processarachidonate secretion
R0050709biological_processnegative regulation of protein secretion
R0050883biological_processmusculoskeletal movement, spinal reflex action
R0051481biological_processnegative regulation of cytosolic calcium ion concentration
R0051584biological_processregulation of dopamine uptake involved in synaptic transmission
R0051898biological_processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
R0051952biological_processregulation of amine transport
R0051967biological_processnegative regulation of synaptic transmission, glutamatergic
R0060134biological_processprepulse inhibition
R0060158biological_processphospholipase C-activating dopamine receptor signaling pathway
R0060161biological_processpositive regulation of dopamine receptor signaling pathway
R1903530biological_processregulation of secretion by cell
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwNLCAISIDRYTaV
ChainResidueDetails
RALA116-VAL132
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues13
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues9
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P18872","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"5-glutamyl histamine","evidences":[{"source":"UniProtKB","id":"P18872","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylcysteine; by pertussis toxin","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"33408414","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues48
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues45
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues41
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues41
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues30
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P62871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"21097933","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues44
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"21097933","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"21097933","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues45
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"21097933","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"21097933","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"21097933","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"21097933","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"21097933","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"21097933","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21097933","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3PBL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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