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2IHB

Crystal structure of the heterodimeric complex of human RGS10 and activated Gi alpha 3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005813cellular_componentcentrosome
A0005834cellular_componentheterotrimeric G-protein complex
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
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
A0007194biological_processnegative regulation of adenylate cyclase activity
A0007212biological_processG protein-coupled dopamine receptor signaling pathway
A0016020cellular_componentmembrane
A0016239biological_processpositive regulation of macroautophagy
A0019001molecular_functionguanyl nucleotide binding
A0019003molecular_functionGDP binding
A0030496cellular_componentmidbody
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0046039biological_processGTP metabolic process
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0070062cellular_componentextracellular exosome
B0001965molecular_functionG-protein alpha-subunit binding
B0005096molecular_functionGTPase activator activity
B0008277biological_processregulation of G protein-coupled receptor signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ALF A 354
ChainResidue
AGLY42
AMG355
AGDP356
AHOH358
AHOH359
AHOH360
AGLU43
ALYS46
AARG178
ALYS180
ATHR181
AVAL201
AGLY203
AGLN204

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 355
ChainResidue
ASER47
ATHR181
AALF354
AGDP356
AHOH359
AHOH360

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 356
ChainResidue
AGLU43
ASER44
AGLY45
ALYS46
ASER47
ATHR48
ASER151
ALEU175
AARG176
ATHR177
AARG178
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
ATHR327
AALF354
AMG355
AHOH359
AHOH360

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER16
ALEU175
AASN269

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CQE5
ChainResidueDetails
BSER33
ATHR181

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:10608901
ChainResidueDetails
BCYS66

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:19478087, ECO:0007744|PDB:2V4Z
ChainResidueDetails
AASP200

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:2IHB, ECO:0007744|PDB:2ODE, ECO:0007744|PDB:2V4Z, ECO:0007744|PDB:4G5O, ECO:0007744|PDB:4G5R
ChainResidueDetails
AALA326

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AARG178

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704
ChainResidueDetails
AGLN204

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250
ChainResidueDetails
ACYS351

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PDB entries from 2024-11-06

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