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5KDL

Crystal structure of the 4 alanine insertion variant of the Gi alpha1 subunit bound to GTPgammaS

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 Residues6
Detailsbinding site for residue MG A 401
ChainResidue
ASER47
ATHR181
AASP200
AGSP402
AHOH501
AHOH502

site_idAC2
Number of Residues25
Detailsbinding site for residue GSP A 402
ChainResidue
AGLY45
ALYS46
ASER47
ATHR48
ASER151
ALEU175
AARG176
ATHR177
AARG178
ATHR181
AGLY202
AGLY203
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
ATHR327
AMG401
AHOH501
AHOH502
AALA41
AGLU43
ASER44

site_idAC3
Number of Residues5
Detailsbinding site for residue MG B 401
ChainResidue
BSER47
BTHR181
BGSP402
BHOH501
BHOH502

site_idAC4
Number of Residues25
Detailsbinding site for residue GSP B 402
ChainResidue
BGLU43
BSER44
BGLY45
BLYS46
BSER47
BTHR48
BASP150
BSER151
BLEU175
BARG176
BTHR177
BARG178
BTHR181
BGLY202
BGLY203
BASN269
BLYS270
BASP272
BLEU273
BCYS325
BALA326
BTHR327
BMG401
BHOH501
BHOH502

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_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 2024-10-30

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