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2G83

Structure of activated G-alpha-i1 bound to a nucleotide-state-selective peptide: Minimal determinants for recognizing the active form of a G protein alpha subunit

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
B0019001molecular_functionguanyl nucleotide binding
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ALF A 357
ChainResidue
AGLY42
AMG356
AGLU43
ALYS46
AARG178
ALYS180
ATHR181
AGLY203
AGLN204
AGDP355

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ALF B 359
ChainResidue
BHOH1
BGLY42
BGLU43
BLYS46
BARG178
BLYS180
BTHR181
BVAL201
BGLY202
BGLY203
BGLN204
BGDP355
BMG358

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 356
ChainResidue
ASER47
AARG178
AVAL179
ATHR181
AGDP355
AALF357

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 358
ChainResidue
BSER47
BVAL179
BTHR181
BGDP355
BALF359

site_idAC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 355
ChainResidue
AHOH2
AHOH13
AGLU43
ASER44
AGLY45
ALYS46
ASER47
ATHR48
ASER151
ALEU175
AARG176
ATHR177
AARG178
ATHR181
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
AMG356
AALF357

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP B 355
ChainResidue
BHOH1
BGLU43
BSER44
BGLY45
BLYS46
BSER47
BTHR48
BSER151
BLEU175
BARG176
BARG178
BTHR181
BASN269
BLYS270
BASP272
BLEU273
BCYS325
BALA326
BMG358
BALF359

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
BSER44
BLYS270

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0
ChainResidueDetails
ATHR48
ATHR182
BTHR48
BTHR182

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
BALA152

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
BARG176

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21115486
ChainResidueDetails
AVAL201
BVAL201

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
BTHR327

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AVAL179
BVAL179

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704
ChainResidueDetails
AARG205
BARG205

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
BTHR181
BGLN204
BGLU43
BARG178

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
BGLN204

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PDB entries from 2024-10-30

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