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2IK8

Crystal structure of the heterodimeric complex of human RGS16 and activated Gi alpha 1

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
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
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
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
A0072678biological_processT cell migration
A1904322biological_processcellular response to forskolin
A1904778biological_processpositive regulation of protein localization to cell cortex
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
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
C0072678biological_processT cell migration
C1904322biological_processcellular response to forskolin
C1904778biological_processpositive regulation of protein localization to cell cortex
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ALF A 355
ChainResidue
AGLY42
AMG356
AGDP401
AHOH408
AHOH416
AHOH417
AGLU43
ALYS46
AARG178
ALYS180
ATHR181
AVAL201
AGLY203
AGLN204

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ALF C 355
ChainResidue
CGLY42
CGLU43
CLYS46
CSER47
CARG178
CVAL179
CLYS180
CTHR181
CGLY203
CGLN204
CMG356
CGDP402
CHOH405
CHOH407
CHOH413

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 356
ChainResidue
ASER47
ATHR181
AALF355
AGDP401
AHOH408
AHOH417

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 356
ChainResidue
CSER47
CTHR181
CALF355
CGDP402
CHOH405
CHOH413

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 357
ChainResidue
AILE93
AASP94
CGLU297

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BILE104
BARG105
BSER106

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 303
ChainResidue
DLYS103
DILE104
DARG105
DSER106

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 357
ChainResidue
AARG105
CHIS322
CPHE323

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 358
ChainResidue
ASER293
AASN294
CARG90

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 359
ChainResidue
ALYS35
APHE199

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 C 358
ChainResidue
CGLN106

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 360
ChainResidue
AHIS213
CGLY217

site_idBC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 401
ChainResidue
AGLU43
ASER44
AGLY45
ALYS46
ASER47
ATHR48
ASER151
ALEU175
AARG176
ATHR177
AARG178
AASN269
ALYS270
AASP272
ACYS325
AALA326
ATHR327
AALF355
AMG356
AHOH405
AHOH408
AHOH417

site_idBC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GDP C 402
ChainResidue
CLEU273
CCYS325
CALA326
CTHR327
CALF355
CMG356
CHOH405
CHOH413
CGLU43
CSER44
CGLY45
CLYS46
CSER47
CTHR48
CASP150
CSER151
CLEU175
CARG176
CTHR177
CARG178
CASN269
CLYS270
CASP272

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:11602604
ChainResidueDetails
BTYR168
DTYR168
CSER44
CLYS270

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:11602604
ChainResidueDetails
BTYR177
DTYR177
CTHR48
CTHR182

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
CALA152

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
CARG176

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21115486
ChainResidueDetails
AVAL201
CVAL201

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
CTHR327

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AVAL179
CVAL179

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704
ChainResidueDetails
AARG205
CARG205

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250
ChainResidueDetails
AGLY352
CGLY352

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
CTHR181
CGLN204
CGLU43
CARG178

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
CGLN204

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PDB entries from 2024-07-24

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