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3SN6

Crystal structure of the beta2 adrenergic receptor-Gs protein complex

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
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
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
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 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
RGLU1011
ALYS211
ACYS237
ASER306
AARG380

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
RASP1020
AASN218

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
RLEU1032
RPHE1104

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
RSER1117
RASN1132

site_idSWS_FT_FI5
Number of Residues23
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
RGLY35-ILE58

site_idSWS_FT_FI6
Number of Residues85
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
RALA59-PHE71
RASP130-ALA150
RARG221-THR274

site_idSWS_FT_FI7
Number of Residues23
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
RILE72-LEU95

site_idSWS_FT_FI8
Number of Residues37
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
RTHR96-CYS106
RARG175-ASN196
RGLN299-LYS305

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
RGLU107-VAL129

site_idSWS_FT_FI10
Number of Residues23
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
RARG151-TYR174

site_idSWS_FT_FI11
Number of Residues23
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
RGLN197-SER220

site_idSWS_FT_FI12
Number of Residues23
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
RLEU275-ILE298

site_idSWS_FT_FI13
Number of Residues23
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
RGLU306-SER329

site_idSWS_FT_FI14
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
ChainResidueDetails
RASP113
RTHR118
RASN293
RASN312
RTYR316

site_idSWS_FT_FI15
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1
ChainResidueDetails
RSER203

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811
ChainResidueDetails
RTYR141

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
RSER246

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
RSER261
RSER262

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000
ChainResidueDetails
RSER345
RSER346

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphoserine; by BARK => ECO:0000305
ChainResidueDetails
RSER355
RSER356

site_idSWS_FT_FI21
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942
ChainResidueDetails
RCYS265

site_idSWS_FT_FI22
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942
ChainResidueDetails
RCYS341

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
RGLU1011proton shuttle (general acid/base)
RASP1020covalent catalysis

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PDB entries from 2024-07-24

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