Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9CBM

Cryo-EM structure of dexmedetomidine-bound alpha-2A-adrenergic receptor in complex with heterotrimeric Gi-protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005834cellular_componentheterotrimeric G-protein complex
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005938cellular_componentcell cortex
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0007198biological_processadenylate cyclase-inhibiting serotonin receptor signaling pathway
A0010854molecular_functionadenylate cyclase regulator activity
A0010855molecular_functionadenylate cyclase inhibitor activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019001molecular_functionguanyl nucleotide binding
A0019003molecular_functionGDP binding
A0030496cellular_componentmidbody
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031749molecular_functionD2 dopamine receptor binding
A0031821molecular_functionG protein-coupled serotonin receptor binding
A0032794molecular_functionGTPase activating protein binding
A0032991cellular_componentprotein-containing complex
A0034695biological_processresponse to prostaglandin E
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0046676biological_processnegative regulation of insulin secretion
A0046872molecular_functionmetal ion binding
A0050805biological_processnegative regulation of synaptic transmission
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0072678biological_processT cell migration
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0099645biological_processneurotransmitter receptor localization to postsynaptic specialization membrane
A1904322biological_processcellular response to forskolin
A1904778biological_processpositive regulation of protein localization to cell cortex
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
R0003824molecular_functioncatalytic activity
R0004930molecular_functionG protein-coupled receptor activity
R0007186biological_processG 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
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SSIvHLCAISLDRYWsI
ChainResidueDetails
RSER134-ILE150

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-119
ALEU175
AASP200
AASN269

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-110

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
RLEU-98
RPHE-26

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
RSER-13
RASN2

site_idSWS_FT_FI5
Number of Residues25
DetailsTRANSMEM: Helical; Name=1 => ECO:0000250
ChainResidueDetails
RLEU49-PHE74

site_idSWS_FT_FI6
Number of Residues187
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
RTHR75-LEU85
RASP145-LYS166

site_idSWS_FT_FI7
Number of Residues25
DetailsTRANSMEM: Helical; Name=2 => ECO:0000250
ChainResidueDetails
RPHE86-MET111

site_idSWS_FT_FI8
Number of Residues43
DetailsTOPO_DOM: Extracellular => ECO:0000250
ChainResidueDetails
RGLY112-CYS121
RGLU188-LYS209
RLEU411-LYS424

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250
ChainResidueDetails
RGLU122-LEU144

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250
ChainResidueDetails
RALA167-ILE187

site_idSWS_FT_FI11
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250
ChainResidueDetails
RTRP210-VAL232

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250
ChainResidueDetails
RVAL390-THR410

site_idSWS_FT_FI13
Number of Residues19
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250
ChainResidueDetails
RPHE425-PHE444

site_idSWS_FT_FI14
Number of Residues1
DetailsSITE: Implicated in ligand binding
ChainResidueDetails
RASP128

site_idSWS_FT_FI15
Number of Residues2
DetailsSITE: Implicated in catechol agonist binding and receptor activation
ChainResidueDetails
RSER215
RSER219

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P22909
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q01338
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails
RCYS457

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 533
ChainResidueDetails
AGLU43electrostatic stabiliser
ATHR48electrostatic stabiliser
AASP200electrostatic stabiliser
AGLN204electrostatic stabiliser

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon