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6PCV

Single Particle Reconstruction of Phosphatidylinositol (3,4,5) trisphosphate-dependent Rac exchanger 1 bound to G protein beta gamma subunits

Functional Information from GO Data
ChainGOidnamespacecontents
A0005085molecular_functionguanyl-nucleotide exchange factor activity
A0005096molecular_functionGTPase activator activity
A0005515molecular_functionprotein binding
A0005543molecular_functionphospholipid binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006801biological_processsuperoxide metabolic process
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0019899molecular_functionenzyme binding
A0030041biological_processactin filament polymerization
A0030217biological_processT cell differentiation
A0030291molecular_functionprotein serine/threonine kinase inhibitor activity
A0030335biological_processpositive regulation of cell migration
A0030426cellular_componentgrowth cone
A0030593biological_processneutrophil chemotaxis
A0030833biological_processregulation of actin filament polymerization
A0032007biological_processnegative regulation of TOR signaling
A0035556biological_processintracellular signal transduction
A0042119biological_processneutrophil activation
A0043198cellular_componentdendritic shaft
A0045321biological_processleukocyte activation
A0045785biological_processpositive regulation of cell adhesion
A0048471cellular_componentperinuclear region of cytoplasm
A0050773biological_processregulation of dendrite development
A0051056biological_processregulation of small GTPase mediated signal transduction
A0072593biological_processreactive oxygen species metabolic process
A1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005834cellular_componentheterotrimeric G-protein complex
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0008283biological_processcell population proliferation
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
G0003924molecular_functionGTPase activity
G0005515molecular_functionprotein binding
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
G0016020cellular_componentmembrane
G0031681molecular_functionG-protein beta-subunit binding
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

site_idPS00741
Number of Residues26
DetailsDH_1 Dbl homology (DH) domain signature. LegYLlsPIqrIcKypLlLkELakrT
ChainResidueDetails
ALEU188-THR213

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER319

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q69ZK0
ChainResidueDetails
ASER1001
ASER1195

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER1200

237735

PDB entries from 2025-06-18

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