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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | cryo-EM structure of l-SPD bound D1R-Gs complex | |||||||||
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Keywords | dopamine receptor / D1R / l-SPD / schizophrenia / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationdopamine neurotransmitter receptor activity, coupled via Gs / cerebral cortex GABAergic interneuron migration / dopamine neurotransmitter receptor activity / Dopamine receptors / dopamine binding / regulation of dopamine uptake involved in synaptic transmission / phospholipase C-activating dopamine receptor signaling pathway / heterotrimeric G-protein binding / 9+0 non-motile cilium / modification of postsynaptic structure ...dopamine neurotransmitter receptor activity, coupled via Gs / cerebral cortex GABAergic interneuron migration / dopamine neurotransmitter receptor activity / Dopamine receptors / dopamine binding / regulation of dopamine uptake involved in synaptic transmission / phospholipase C-activating dopamine receptor signaling pathway / heterotrimeric G-protein binding / 9+0 non-motile cilium / modification of postsynaptic structure / sensory perception of chemical stimulus / adult walking behavior / positive regulation of potassium ion transport / G protein-coupled receptor complex / mu-type opioid receptor binding / corticotropin-releasing hormone receptor 1 binding / arrestin family protein binding / non-motile cilium / G protein-coupled dopamine receptor signaling pathway / beta-2 adrenergic receptor binding / mating behavior / ciliary membrane / dopamine metabolic process / adenylate cyclase-activating G protein-coupled bile acid receptor signaling pathway / adenylate cyclase-activating serotonin receptor signaling pathway / intracellular transport / regulation of skeletal muscle contraction / transmission of nerve impulse / hair follicle placode formation / developmental growth / PKA activation in glucagon signalling / renal water homeostasis / G-protein alpha-subunit binding / D1 dopamine receptor binding / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / vascular endothelial cell response to laminar fluid shear stress / Hedgehog 'off' state / activation of adenylate cyclase activity / adenylate cyclase-activating adrenergic receptor signaling pathway / insulin-like growth factor receptor binding / cellular response to acidic pH / positive regulation of synaptic transmission, glutamatergic / synapse assembly / ovarian follicle development / cellular response to glucagon stimulus / visual learning / presynaptic modulation of chemical synaptic transmission / ionotropic glutamate receptor binding / intracellular glucose homeostasis / positive regulation of release of sequestered calcium ion into cytosol / adenylate cyclase activator activity / positive regulation of insulin secretion involved in cellular response to glucose stimulus / positive regulation of insulin secretion / trans-Golgi network membrane / bone development / negative regulation of inflammatory response to antigenic stimulus / response to prostaglandin E / vasodilation / GABA-ergic synapse / platelet aggregation / cognition / G protein-coupled receptor activity / G-protein beta/gamma-subunit complex binding / Olfactory Signaling Pathway / Activation of the phototransduction cascade / sensory perception of smell / G protein-coupled acetylcholine receptor signaling pathway / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / G-protein activation / Glucagon signaling in metabolic regulation / G beta:gamma signalling through CDC42 / Prostacyclin signalling through prostacyclin receptor / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / photoreceptor disc membrane / G beta:gamma signalling through BTK / ADP signalling through P2Y purinoceptor 12 / Sensory perception of sweet, bitter, and umami (glutamate) taste / Glucagon-type ligand receptors / Adrenaline,noradrenaline inhibits insulin secretion / cilium / Vasopressin regulates renal water homeostasis via Aquaporins / G alpha (z) signalling events / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / ADP signalling through P2Y purinoceptor 1 / cellular response to catecholamine stimulus / G beta:gamma signalling through PI3Kgamma / ADORA2B mediated anti-inflammatory cytokines production / adenylate cyclase-activating dopamine receptor signaling pathway / cellular response to prostaglandin E stimulus / positive regulation of cold-induced thermogenesis / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / heterotrimeric G-protein complex / G alpha (12/13) signalling events / Inactivation, recovery and regulation of the phototransduction cascade / G-protein beta-subunit binding Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) / ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.49 Å | |||||||||
Authors | Zhang XY / Liu H / Zhuang YW / Xu HE | |||||||||
| Funding support | China, 1 items
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Citation | Journal: To Be PublishedTitle: cryo-EM structure of l-SPD binding to D2R Authors: Zhang XY / Liu H / Zhuang YW | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_63870.map.gz | 59.8 MB | EMDB map data format | |
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| Header (meta data) | emd-63870-v30.xml emd-63870.xml | 19 KB 19 KB | Display Display | EMDB header |
| Images | emd_63870.png | 40.5 KB | ||
| Masks | emd_63870_msk_1.map | 64 MB | Mask map | |
| Filedesc metadata | emd-63870.cif.gz | 6.5 KB | ||
| Others | emd_63870_half_map_1.map.gz emd_63870_half_map_2.map.gz | 59.4 MB 59.4 MB | ||
| Archive directory | https://data.pdbj.org/pub/emdb/structures/EMD-63870 ftp://data.pdbj.org/pub/emdb/structures/EMD-63870 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9u5eMC ![]() 9u5fC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_63870.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.81 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_63870_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_63870_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_63870_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : cryo-EM structure of l-SPD bound D1R-Gs complex
| Entire | Name: cryo-EM structure of l-SPD bound D1R-Gs complex |
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| Components |
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-Supramolecule #1: cryo-EM structure of l-SPD bound D1R-Gs complex
| Supramolecule | Name: cryo-EM structure of l-SPD bound D1R-Gs complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Guanine nucleotide-binding protein G(s) subunit alpha isoforms sh...
| Macromolecule | Name: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO EC number: Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 28.790529 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: GGSGGSMTED QRNEEKAQRE ANKMIEKQLQ KDKQVYRATH RLLLLGADNS GKSTIVKQMR IYHVNSGIFE TKFQVDKVNF HMFDVGAQR DERRKWIQCF NDVTAIIFVV DSSDYNRLQE ALNDFKSIWN NRWLRTISVI LFLNKQDLLA EKVLAGKSKI E DYFPEFAR ...String: GGSGGSMTED QRNEEKAQRE ANKMIEKQLQ KDKQVYRATH RLLLLGADNS GKSTIVKQMR IYHVNSGIFE TKFQVDKVNF HMFDVGAQR DERRKWIQCF NDVTAIIFVV DSSDYNRLQE ALNDFKSIWN NRWLRTISVI LFLNKQDLLA EKVLAGKSKI E DYFPEFAR YTTPEDATPE PGEDPRVTRA KYFIRDEFLR ISTASGDGRH YCYPHFTCSV DTENARRIFN DCRDIIQRMH LR QYELL UniProtKB: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas |
-Macromolecule #2: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
| Macromolecule | Name: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 37.915496 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MGSLLQSELD QLRQEAEQLK NQIRDARKAC ADATLSQITN NIDPVGRIQM RTRRTLRGHL AKIYAMHWGT DSRLLVSASQ DGKLIIWDS YTTNKVHAIP LRSSWVMTCA YAPSGNYVAC GGLDNICSIY NLKTREGNVR VSRELAGHTG YLSCCRFLDD N QIVTSSGD ...String: MGSLLQSELD QLRQEAEQLK NQIRDARKAC ADATLSQITN NIDPVGRIQM RTRRTLRGHL AKIYAMHWGT DSRLLVSASQ DGKLIIWDS YTTNKVHAIP LRSSWVMTCA YAPSGNYVAC GGLDNICSIY NLKTREGNVR VSRELAGHTG YLSCCRFLDD N QIVTSSGD TTCALWDIET GQQTTTFTGH TGDVMSLSLA PDTRLFVSGA CDASAKLWDV REGMCRQTFT GHESDINAIC FF PNGNAFA TGSDDATCRL FDLRADQELM TYSHDNIICG ITSVSFSKSG RLLLAGYDDF NCNVWDALKA DRAGVLAGHD NRV SCLGVT DDGMAVATGS WDSFLKIWN UniProtKB: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 |
-Macromolecule #3: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
| Macromolecule | Name: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 7.861143 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP FREKKFFCAI L UniProtKB: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 |
-Macromolecule #4: Nanobody35
| Macromolecule | Name: Nanobody35 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 15.271938 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MQVQLQESGG GLVQPGGSLR LSCAASGFTF SNYKMNWVRQ APGKGLEWVS DISQSGASIS YTGSVKGRFT ISRDNAKNTL YLQMNSLKP EDTAVYYCAR CPAPFTRDCF DVTSTTYAYR GQGTQVTVSS HHHHHHEPEA |
-Macromolecule #5: D(1A) dopamine receptor
| Macromolecule | Name: D(1A) dopamine receptor / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 49.339168 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MRTLNTSAMD GTGLVVERDF SVRILTACFL SLLILSTLLG NTLVCAAVIR FRHLRSKVTN FFVISLAVSD LLVAVLVMPW KAVAEIAGF WPFGSFCNIW VAFDIMCSTA SILNLCVISV DRYWAISSPF RYERKMTPKA AFILISVAWT LSVLISFIPV Q LSWHKAKP ...String: MRTLNTSAMD GTGLVVERDF SVRILTACFL SLLILSTLLG NTLVCAAVIR FRHLRSKVTN FFVISLAVSD LLVAVLVMPW KAVAEIAGF WPFGSFCNIW VAFDIMCSTA SILNLCVISV DRYWAISSPF RYERKMTPKA AFILISVAWT LSVLISFIPV Q LSWHKAKP TSPSDGNATS LAETIDNCDS SLSRTYAISS SVISFYIPVA IMIVTYTRIY RIAQKQIRRI AALERAAVHA KN CQTTTGN GKPVECSQPE SSFKMSFKRE TKVLKTLSVI MGVFVCCWLP FFILNCILPF CGSGETQPFC IDSNTFDVFV WFG WANSSL NPIIYAFNAD FRKAFSTLLG CYRLCPATNN AIETVSINNN GAAMFSSHHE PRGSISKECN LVYLIPHAVG SSED LKKEE AAGIARPLEK LSPALSVILD YDTDVSLEKI QPITQNGQHP T UniProtKB: D(1A) dopamine receptor |
-Macromolecule #6: (13~{a}~{S})-3,9-dimethoxy-6,8,13,13~{a}-tetrahydro-5~{H}-isoquin...
| Macromolecule | Name: (13~{a}~{S})-3,9-dimethoxy-6,8,13,13~{a}-tetrahydro-5~{H}-isoquinolino[2,1-b]isoquinoline-2,10-diol type: ligand / ID: 6 / Number of copies: 1 / Formula: A1EN9 |
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| Molecular weight | Theoretical: 327.374 Da |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TALOS ARCTICA |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: DARK FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
China, 1 items
Citation
























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Y (Row.)
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Processing
FIELD EMISSION GUN
