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8DCR

Cryo-EM structure of dobutamine-bound beta1-adrenergic receptor in complex with heterotrimeric Gs-protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005834cellular_componentheterotrimeric G-protein complex
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
A0007606biological_processsensory perception of chemical stimulus
A0010856molecular_functionadenylate cyclase activator activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031698molecular_functionbeta-2 adrenergic receptor binding
A0031748molecular_functionD1 dopamine receptor binding
A0031852molecular_functionmu-type opioid receptor binding
A0035255molecular_functionionotropic glutamate receptor binding
A0046872molecular_functionmetal ion binding
A0051430molecular_functioncorticotropin-releasing hormone receptor 1 binding
A0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005834cellular_componentheterotrimeric G-protein complex
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0008283biological_processcell population proliferation
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
G0003924molecular_functionGTPase activity
G0005515molecular_functionprotein binding
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
G0016020cellular_componentmembrane
G0031681molecular_functionG-protein beta-subunit binding
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
R0003796molecular_functionlysozyme activity
R0004930molecular_functionG protein-coupled receptor activity
R0007186biological_processG protein-coupled receptor signaling pathway
R0009253biological_processpeptidoglycan catabolic process
R0016020cellular_componentmembrane
R0016798molecular_functionhydrolase activity, acting on glycosyl bonds
R0016998biological_processcell wall macromolecule catabolic process
R0030430cellular_componenthost cell cytoplasm
R0031640biological_processkilling of cells of another organism
R0042742biological_processdefense response to bacterium
R0044659biological_processviral release from host cell by cytolysis
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAIDRYLaI
ChainResidueDetails
RALA127-ILE143

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 Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
RGLU-121
ALYS197
ACYS223
ASER292
AARG366

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
RASP-112
AASN204

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
RLEU-100
RPHE-28

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
RSER-15
RASN0

site_idSWS_FT_FI5
Number of Residues28
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
RGLN39-GLY67

site_idSWS_FT_FI6
Number of Residues78
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18594507
ChainResidueDetails
RSER68-THR76
RASP138-ARG155
RARG232-VAL320

site_idSWS_FT_FI7
Number of Residues26
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
RASN77-VAL103

site_idSWS_FT_FI8
Number of Residues40
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:18594507
ChainResidueDetails
RARG104-GLU115
RHIS180-ARG205
RLYS351-ARG355

site_idSWS_FT_FI9
Number of Residues21
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
RLEU116-ILE137

site_idSWS_FT_FI10
Number of Residues23
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
RALA156-MET179

site_idSWS_FT_FI11
Number of Residues25
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
RALA206-TYR231

site_idSWS_FT_FI12
Number of Residues29
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
RPRO321-ARG350

site_idSWS_FT_FI13
Number of Residues22
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
RLEU356-HIS378

site_idSWS_FT_FI14
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4
ChainResidueDetails
RASP121
RSER211
RASP364

site_idSWS_FT_FI15
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
RGLU-121proton shuttle (general acid/base)
RASP-112covalent catalysis

229183

PDB entries from 2024-12-18

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