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6M8H

Crystal Structure of the R208Q mutant of G(i) subunit alpha-1

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
Functional Information from PDB Data
site_idAC1
Number of Residues30
Detailsbinding site for residue GSP A 401
ChainResidue
AGLY42
AARG176
ATHR177
AARG178
ATHR181
AGLY202
AGLY203
AASN269
ALYS270
AASP272
ALEU273
AGLU43
ACYS325
AALA326
ATHR327
AMG402
AHOH514
AHOH528
AHOH536
AHOH553
AHOH566
AHOH579
ASER44
AHOH617
AGLY45
ALYS46
ASER47
ATHR48
ASER151
ALEU175

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 402
ChainResidue
ASER47
ATHR181
AASP200
AGSP401
AHOH514
AHOH528

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, 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
AGLU43
ALEU175
AASP200
AASN269

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:4PAO
ChainResidueDetails
ASER47

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:1GIL, ECO:0007744|PDB:4N0D
ChainResidueDetails
AASP150

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
ATHR181

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
AALA326

site_idSWS_FT_FI6
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:26253820
ChainResidueDetails
AGLY2

site_idSWS_FT_FI7
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:26253820
ChainResidueDetails
ACYS3

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 533
ChainResidueDetails
AGLU43electrostatic stabiliser
ATHR48electrostatic stabiliser
AARG178electrostatic stabiliser
AASP200electrostatic stabiliser
AGLN204electrostatic stabiliser

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PDB entries from 2024-11-13

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