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1Y3A

Structure of G-Alpha-I1 bound to a GDP-selective peptide provides insight into guanine nucleotide exchange

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005813cellular_componentcentrosome
A0005834cellular_componentheterotrimeric G-protein complex
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005938cellular_componentcell cortex
A0007049biological_processcell cycle
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
A0016020cellular_componentmembrane
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
A0043434biological_processresponse to peptide hormone
A0043949biological_processregulation of cAMP-mediated signaling
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0070062cellular_componentextracellular exosome
A1904322biological_processcellular response to forskolin
A1904778biological_processpositive regulation of protein localization to cell cortex
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0001664molecular_functionG protein-coupled receptor binding
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005813cellular_componentcentrosome
B0005834cellular_componentheterotrimeric G-protein complex
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0005938cellular_componentcell cortex
B0007049biological_processcell cycle
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
B0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
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
B0043434biological_processresponse to peptide hormone
B0043949biological_processregulation of cAMP-mediated signaling
B0046872molecular_functionmetal ion binding
B0051301biological_processcell division
B0060236biological_processregulation of mitotic spindle organization
B0070062cellular_componentextracellular exosome
B1904322biological_processcellular response to forskolin
B1904778biological_processpositive regulation of protein localization to cell cortex
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0001664molecular_functionG protein-coupled receptor binding
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005765cellular_componentlysosomal membrane
C0005813cellular_componentcentrosome
C0005834cellular_componentheterotrimeric G-protein complex
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0005938cellular_componentcell cortex
C0007049biological_processcell cycle
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
C0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
C0016020cellular_componentmembrane
C0019001molecular_functionguanyl nucleotide binding
C0019003molecular_functionGDP binding
C0030496cellular_componentmidbody
C0031683molecular_functionG-protein beta/gamma-subunit complex binding
C0031749molecular_functionD2 dopamine receptor binding
C0031821molecular_functionG protein-coupled serotonin receptor binding
C0043434biological_processresponse to peptide hormone
C0043949biological_processregulation of cAMP-mediated signaling
C0046872molecular_functionmetal ion binding
C0051301biological_processcell division
C0060236biological_processregulation of mitotic spindle organization
C0070062cellular_componentextracellular exosome
C1904322biological_processcellular response to forskolin
C1904778biological_processpositive regulation of protein localization to cell cortex
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0001664molecular_functionG protein-coupled receptor binding
D0003924molecular_functionGTPase activity
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005730cellular_componentnucleolus
D0005737cellular_componentcytoplasm
D0005765cellular_componentlysosomal membrane
D0005813cellular_componentcentrosome
D0005834cellular_componentheterotrimeric G-protein complex
D0005856cellular_componentcytoskeleton
D0005886cellular_componentplasma membrane
D0005938cellular_componentcell cortex
D0007049biological_processcell cycle
D0007165biological_processsignal transduction
D0007186biological_processG protein-coupled receptor signaling pathway
D0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
D0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
D0016020cellular_componentmembrane
D0019001molecular_functionguanyl nucleotide binding
D0019003molecular_functionGDP binding
D0030496cellular_componentmidbody
D0031683molecular_functionG-protein beta/gamma-subunit complex binding
D0031749molecular_functionD2 dopamine receptor binding
D0031821molecular_functionG protein-coupled serotonin receptor binding
D0043434biological_processresponse to peptide hormone
D0043949biological_processregulation of cAMP-mediated signaling
D0046872molecular_functionmetal ion binding
D0051301biological_processcell division
D0060236biological_processregulation of mitotic spindle organization
D0070062cellular_componentextracellular exosome
D1904322biological_processcellular response to forskolin
D1904778biological_processpositive regulation of protein localization to cell cortex
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP A 355
ChainResidue
AGLY42
AARG176
AARG178
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
ATHR327
AHOH358
AGLU43
AHOH372
ASER44
AGLY45
ALYS46
ASER47
ATHR48
AASP150
ALEU175

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP B 356
ChainResidue
BGLU43
BSER44
BGLY45
BLYS46
BSER47
BTHR48
BASP150
BLEU175
BARG176
BTHR177
BARG178
BASN269
BLYS270
BASP272
BLEU273
BCYS325
BALA326
BTHR327
BHOH358
BHOH365
BHOH366

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP C 357
ChainResidue
CGLY42
CGLU43
CSER44
CGLY45
CLYS46
CSER47
CTHR48
CASP150
CLEU175
CARG176
CTHR177
CARG178
CASN269
CLYS270
CASP272
CLEU273
CCYS325
CALA326
CTHR327
CHOH362
CHOH367

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP D 358
ChainResidue
DGLY42
DGLU43
DSER44
DGLY45
DLYS46
DSER47
DTHR48
DASP150
DLEU175
DARG176
DTHR177
DARG178
DASN269
DLYS270
DASP272
DLEU273
DCYS325
DALA326
DTHR327
DHOH372
DHOH374

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:21115486, ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q
ChainResidueDetails
ASER44
ALYS270
BSER44
BLYS270
CSER44
CLYS270
DSER44
DLYS270

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0
ChainResidueDetails
ATHR48
ATHR182
BTHR48
BTHR182
CTHR48
CTHR182
DTHR48
DTHR182

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:4G5Q
ChainResidueDetails
AALA152
BALA152
CALA152
DALA152

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q
ChainResidueDetails
AARG176
BARG176
CARG176
DARG176

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21115486
ChainResidueDetails
AVAL201
BVAL201
CVAL201
DVAL201

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q
ChainResidueDetails
ATHR327
BTHR327
CTHR327
DTHR327

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AVAL179
BVAL179
CVAL179
DVAL179

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704
ChainResidueDetails
AARG205
BARG205
CARG205
DARG205

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250
ChainResidueDetails
AGLY352
BGLY352
CGLY352
DGLY352

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PDB entries from 2024-03-27

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