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1GP2

G PROTEIN HETEROTRIMER GI_ALPHA_1 BETA_1 GAMMA_2 WITH GDP BOUND

Functional Information from GO Data
ChainGOidnamespacecontents
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
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 355
ChainResidue
AALA41
AARG176
AARG178
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
ATHR327
AHOH380
AGLU43
AHOH461
AHOH466
AHOH561
ASER44
AGLY45
ALYS46
ASER47
ATHR48
AASP150
ASER151

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:0000269|PubMed:7626050
ChainResidueDetails
GSER3
AARG176
AVAL201
ALYS270

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000269|PubMed:1903391
ChainResidueDetails
GALA69

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000269|PubMed:12764189, ECO:0000269|PubMed:1903391, ECO:0000269|PubMed:7626050
ChainResidueDetails
GALA69

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19703466, ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:4PAO
ChainResidueDetails
ATHR182

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1GIA, ECO:0007744|PDB:1GIL, ECO:0007744|PDB:3FFA, ECO:0007744|PDB:4N0D, ECO:0007744|PDB:4PAO, ECO:0007744|PDB:4PAQ
ChainResidueDetails
ATHR327

site_idSWS_FT_FI6
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:26253820
ChainResidueDetails
ACYS3

site_idSWS_FT_FI7
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:26253820
ChainResidueDetails
ATHR4

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
ATHR181
AGLN204
AGLU43
AARG178

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLN204

site_idMCSA1
Number of Residues5
DetailsM-CSA 533
ChainResidueDetails
ASER44electrostatic stabiliser
AILE49electrostatic stabiliser
AVAL179electrostatic stabiliser
AVAL201electrostatic stabiliser
AARG205electrostatic stabiliser

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PDB entries from 2024-11-13

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