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3ONW

Structure of a G-alpha-i1 mutant with enhanced affinity for the RGS14 GoLoco motif.

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
C0005096molecular_functionGTPase activator activity
C0030695molecular_functionGTPase regulator activity
D0005096molecular_functionGTPase activator activity
D0030695molecular_functionGTPase regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GDP A 401
ChainResidue
AALA41
AARG176
AARG178
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
ATHR327
CARG516
AGLU43
ASER44
AGLY45
ALYS46
ASER47
ATHR48
AASP150
ASER151

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP B 401
ChainResidue
BHOH23
BALA41
BGLU43
BSER44
BGLY45
BLYS46
BSER47
BTHR48
BASP150
BSER151
BARG176
BARG178
BASN269
BLYS270
BASP272
BLEU273
BCYS325
BALA326
BTHR327
BHOH357
DARG516

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1
ChainResidue
BTYR154
BGLN172
BARG176
BHOH365

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2
ChainResidue
BARG242
DSER510
DGLY511

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
ASER293
AASN294

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
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
AGLU43
AASN269
BGLU43
BASN269

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0
ChainResidueDetails
ASER47
ATHR181
BSER47
BTHR181

site_idSWS_FT_FI3
Number of Residues2
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
ASER151
BSER151

site_idSWS_FT_FI4
Number of Residues2
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
ALEU175
BLEU175

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21115486
ChainResidueDetails
AASP200
BASP200

site_idSWS_FT_FI6
Number of Residues2
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
AALA326
BALA326

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AARG178
BARG178

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704
ChainResidueDetails
AGLN204
BGLN204

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250
ChainResidueDetails
ACYS351
BCYS351

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건을2024-03-27부터공개중

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