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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3SN6

Crystal structure of the beta2 adrenergic receptor-Gs protein complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
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
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
R0003824molecular_functioncatalytic activity
R0004930molecular_functionG protein-coupled receptor activity
R0004941molecular_functionbeta2-adrenergic receptor activity
R0006940biological_processregulation of smooth muscle contraction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0009253biological_processpeptidoglycan catabolic process
R0016020cellular_componentmembrane
R0016787molecular_functionhydrolase activity
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
R0097746biological_processblood vessel diameter maintenance
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE P0G R 366
ChainResidue
RTRP109
RASN293
RTYR308
RASN312
RTHR110
RASP113
RVAL117
RPHE193
RSER203
RSER204
RSER207
RPHE290
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAVDRYFaI
ChainResidueDetails
RALA119-ILE135
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 Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}
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":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P62871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues32
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues16
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3D4S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17952055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RH1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8521811","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"27481942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2540197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27481942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails

238582

PDB entries from 2025-07-09

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