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8UUJ

CryoEM Structure of HCA2 DREADD Gi1 in complex with FCH-2296413

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
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005794cellular_componentGolgi apparatus
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
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0007198biological_processadenylate cyclase-inhibiting serotonin receptor signaling pathway
A0007218biological_processneuropeptide signaling pathway
A0010854molecular_functionadenylate cyclase regulator activity
A0010855molecular_functionadenylate cyclase inhibitor activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
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
A0034451cellular_componentcentriolar satellite
A0034695biological_processresponse to prostaglandin E
A0036064cellular_componentciliary basal body
A0043434biological_processresponse to peptide hormone
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0046676biological_processnegative regulation of insulin secretion
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0070062cellular_componentextracellular exosome
A0070098biological_processchemokine-mediated signaling pathway
A0072678biological_processT cell migration
A1901082biological_processpositive regulation of relaxation of smooth muscle
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
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
C0005515molecular_functionprotein binding
C0005834cellular_componentheterotrimeric G-protein complex
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
C0016020cellular_componentmembrane
C0031681molecular_functionG-protein beta-subunit binding
C0045202cellular_componentsynapse
C0048144biological_processfibroblast proliferation
C0070062cellular_componentextracellular exosome
C0071380biological_processcellular response to prostaglandin E stimulus
C0071870biological_processcellular response to catecholamine stimulus
R0001614molecular_functionpurinergic nucleotide receptor activity
R0004930molecular_functionG protein-coupled receptor activity
R0005525molecular_functionGTP binding
R0005886cellular_componentplasma membrane
R0006915biological_processapoptotic process
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
R0033031biological_processpositive regulation of neutrophil apoptotic process
R0035590biological_processpurinergic nucleotide receptor signaling pathway
R0050995biological_processnegative regulation of lipid catabolic process
R0070165biological_processpositive regulation of adiponectin secretion
R0070553molecular_functionnicotinic acid receptor activity
Functional Information from PROSITE/UniProt
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
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
CALA2
RASP82-ARG98
RTHR162-MET189
RARG248-ASP270

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
CCYS68
ATHR181

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
CCYS68
RVAL120-THR140
RSER211-ALA226
RTYR292-ARG360

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
RILE61-THR81

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
RVAL99-ALA119

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
RALA141-TYR161

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
RPHE190-TRP210

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RILE227-VAL247

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RLEU271-TYR291

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
RSER325

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824
ChainResidueDetails
ACYS3

237423

PDB entries from 2025-06-11

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