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8THL

Cryo-EM structure of epinephrine-bound alpha-1A-adrenergic receptor in complex with heterotrimeric Gq-protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007186biological_processG protein-coupled receptor signaling pathway
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
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
B0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
B0007265biological_processRas protein signal transduction
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
B0070062cellular_componentextracellular exosome
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
B1903561cellular_componentextracellular vesicle
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
G0048144biological_processfibroblast proliferation
G0070062cellular_componentextracellular exosome
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. ASImGLCIISIDRYIgV
ChainResidueDetails
RALA112-VAL128

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-139

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-130

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
RLEU-118
RPHE-46

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
RSER-33
RASN-18

site_idSWS_FT_FI5
Number of Residues23
DetailsTRANSMEM: Helical; Name=1 => ECO:0000250
ChainResidueDetails
RLEU28-VAL51
AASP85
ALEU154
AALA218

site_idSWS_FT_FI6
Number of Residues99
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
RALA52-TYR64
RASP123-GLY143
RARG206-PHE301

site_idSWS_FT_FI7
Number of Residues23
DetailsTRANSMEM: Helical; Name=2 => ECO:0000250
ChainResidueDetails
RILE65-VAL88

site_idSWS_FT_FI8
Number of Residues30
DetailsTOPO_DOM: Extracellular => ECO:0000250
ChainResidueDetails
RLEU89-CYS99
RPRO168-GLU181
RTYR326-PHE333

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250
ChainResidueDetails
RASN100-ILE122

site_idSWS_FT_FI10
Number of Residues23
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250
ChainResidueDetails
RLEU144-GLN167

site_idSWS_FT_FI11
Number of Residues23
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250
ChainResidueDetails
RPRO182-CYS205

site_idSWS_FT_FI12
Number of Residues23
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250
ChainResidueDetails
RLYS302-ILE325

site_idSWS_FT_FI13
Number of Residues23
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250
ChainResidueDetails
RLYS334-PHE357

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
RSER215

site_idSWS_FT_FI15
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN22

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
RGLU-139proton shuttle (general acid/base)
RASP-130covalent catalysis

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PDB entries from 2024-07-24

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