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2ZJZ

Structure of the K349P mutant of Gi alpha 1 subunit bound to GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
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
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
A0043949biological_processregulation of cAMP-mediated signaling
A0046872molecular_functionmetal ion binding
A0050805biological_processnegative regulation of synaptic transmission
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
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
B0000287molecular_functionmagnesium ion binding
B0001664molecular_functionG protein-coupled receptor binding
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005834cellular_componentheterotrimeric G-protein complex
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0005938cellular_componentcell cortex
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
B0016787molecular_functionhydrolase activity
B0019001molecular_functionguanyl nucleotide binding
B0019003molecular_functionGDP binding
B0030496cellular_componentmidbody
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0031749molecular_functionD2 dopamine receptor binding
B0031821molecular_functionG protein-coupled serotonin receptor binding
B0032794molecular_functionGTPase activating protein binding
B0032991cellular_componentprotein-containing complex
B0043949biological_processregulation of cAMP-mediated signaling
B0046872molecular_functionmetal ion binding
B0050805biological_processnegative regulation of synaptic transmission
B0051301biological_processcell division
B0060236biological_processregulation of mitotic spindle organization
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0099645biological_processneurotransmitter receptor localization to postsynaptic specialization membrane
B1904322biological_processcellular response to forskolin
B1904778biological_processpositive regulation of protein localization to cell cortex
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GDP A 355
ChainResidue
AGLY42
AARG176
ATHR177
AARG178
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
ATHR327
AGLU43
ASER44
AGLY45
ALYS46
ASER47
ATHR48
ASER151
ALEU175

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP B 355
ChainResidue
BALA41
BGLY42
BGLU43
BSER44
BGLY45
BLYS46
BSER47
BTHR48
BASP150
BSER151
BLEU175
BARG176
BTHR177
BARG178
BASN269
BLYS270
BASP272
BLEU273
BCYS325
BALA326
BTHR327

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
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
BGLU43
BLEU175
BASP200
BASN269

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:4PAO
ChainResidueDetails
ASER47
BSER47

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:1GIL, ECO:0007744|PDB:4N0D
ChainResidueDetails
AASP150
BASP150

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19703466, ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:4PAO
ChainResidueDetails
ATHR181
BTHR181

site_idSWS_FT_FI5
Number of Residues2
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
BALA326

site_idSWS_FT_FI6
Number of Residues2
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:26253820
ChainResidueDetails
AGLY2
BGLY2

site_idSWS_FT_FI7
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:26253820
ChainResidueDetails
ACYS3
BCYS3

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
ATHR181
AGLU43
AARG178

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BTHR181
BGLN204
BGLU43
BARG178

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BGLN204

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

site_idMCSA2
Number of Residues5
DetailsM-CSA 533
ChainResidueDetails
BGLU43electrostatic stabiliser
BTHR48electrostatic stabiliser
BARG178electrostatic stabiliser
BASP200electrostatic stabiliser
BGLN204electrostatic stabiliser

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PDB entries from 2024-09-25

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