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1KJY

Crystal Structure of Human G[alpha]i1 Bound to the GoLoco Motif of RGS14

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
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
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
A0034695biological_processresponse to prostaglandin E
A0043434biological_processresponse to peptide hormone
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0070062cellular_componentextracellular exosome
A0072678biological_processT cell migration
A1904322biological_processcellular response to forskolin
A1904778biological_processpositive regulation of protein localization to cell cortex
B0005096molecular_functionGTPase activator activity
B0030695molecular_functionGTPase regulator activity
C0000287molecular_functionmagnesium ion binding
C0001664molecular_functionG protein-coupled receptor binding
C0003924molecular_functionGTPase activity
C0003925molecular_functionG protein activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005765cellular_componentlysosomal membrane
C0005813cellular_componentcentrosome
C0005829cellular_componentcytosol
C0005834cellular_componentheterotrimeric G-protein complex
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0005938cellular_componentcell cortex
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
C0007198biological_processadenylate cyclase-inhibiting serotonin receptor signaling pathway
C0010854molecular_functionadenylate cyclase regulator activity
C0016787molecular_functionhydrolase activity
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
C0034695biological_processresponse to prostaglandin E
C0043434biological_processresponse to peptide hormone
C0045542biological_processpositive regulation of cholesterol biosynthetic process
C0046872molecular_functionmetal ion binding
C0051301biological_processcell division
C0060236biological_processregulation of mitotic spindle organization
C0070062cellular_componentextracellular exosome
C0072678biological_processT cell migration
C1904322biological_processcellular response to forskolin
C1904778biological_processpositive regulation of protein localization to cell cortex
D0005096molecular_functionGTPase activator activity
D0030695molecular_functionGTPase regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 800
ChainResidue
AGDP356
BSER510
BHIS513
BARG516
BHOH4085

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 801
ChainResidue
CGDP355
CSER1047
CASP1200

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS C 802
ChainResidue
CSER1143
CPHE1140

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS A 803
ChainResidue
APHE140
ASER143

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CS A 804
ChainResidue
AASP158

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS C 805
ChainResidue
CHIS1057
CTHR1190

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS C 806
ChainResidue
CASN1157
CASP1158

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CS D 807
ChainResidue
DASP1496

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS A 808
ChainResidue
AALA59
ATYR61

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS C 809
ChainResidue
CLYS1092
CASP1094

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CS A 811
ChainResidue
AHIS188

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS A 812
ChainResidue
AHIS57
ATHR190

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CS A 813
ChainResidue
AGLU186

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CS C 814
ChainResidue
CHIS1188

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS C 815
ChainResidue
CGLU1186
CHOH4001

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS A 816
ChainResidue
APHE95
AGLY96

site_idBC8
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP C 355
ChainResidue
CMG801
CGLY1042
CGLU1043
CSER1044
CGLY1045
CLYS1046
CSER1047
CTHR1048
CSER1151
CARG1176
CARG1178
CASN1269
CLYS1270
CASP1272
CLEU1273
CCYS1325
CALA1326
CTHR1327
CHOH4178
DARG1516

site_idBC9
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP A 356
ChainResidue
AGLY42
AGLU43
ASER44
AGLY45
ALYS46
ASER47
ATHR48
ASER151
AARG176
AARG178
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
ATHR327
AHOH4043
BARG516
BMG800

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
ASER44
ALYS270
CSER1044
CLYS1270

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0
ChainResidueDetails
ATHR48
ATHR182
CTHR1048
CTHR1182

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
AALA152
CALA1152

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
AARG176
CARG1176

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21115486
ChainResidueDetails
AVAL201
CVAL1201

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
ATHR327
CTHR1327

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AVAL179
CVAL1179

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704
ChainResidueDetails
AARG205
CARG1205

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250
ChainResidueDetails
AGLY352
CGLY1352

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
ATHR181
AGLN204
AGLU43
AARG178

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
CGLU1043
CGLN1204
CARG1178
CTHR1181

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLN204

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
CGLN1204

227111

PDB entries from 2024-11-06

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