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4QJ3

Structure of a fragment of human phospholipase C-beta3 delta472-559, in complex with Galphaq

Functional Information from GO Data
ChainGOidnamespacecontents
A0001501biological_processskeletal system development
A0001508biological_processaction potential
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005794cellular_componentGolgi apparatus
A0005834cellular_componentheterotrimeric G-protein complex
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
A0007207biological_processphospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway
A0007215biological_processglutamate receptor signaling pathway
A0007507biological_processheart development
A0008217biological_processregulation of blood pressure
A0009791biological_processpost-embryonic development
A0010543biological_processregulation of platelet activation
A0016020cellular_componentmembrane
A0016322biological_processneuron remodeling
A0016787molecular_functionhydrolase activity
A0019001molecular_functionguanyl nucleotide binding
A0021884biological_processforebrain neuron development
A0030234molecular_functionenzyme regulator activity
A0030425cellular_componentdendrite
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031965cellular_componentnuclear membrane
A0032024biological_processpositive regulation of insulin secretion
A0042711biological_processmaternal behavior
A0042733biological_processembryonic digit morphogenesis
A0044297cellular_componentcell body
A0045202cellular_componentsynapse
A0045634biological_processregulation of melanocyte differentiation
A0046872molecular_functionmetal ion binding
A0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
A0048066biological_processdevelopmental pigmentation
A0060158biological_processphospholipase C-activating dopamine receptor signaling pathway
A0086100biological_processendothelin receptor signaling pathway
A0099105biological_procession channel modulating, G protein-coupled receptor signaling pathway
A1904888biological_processcranial skeletal system development
A1990806biological_processligand-gated ion channel signaling pathway
B0004435molecular_functionphosphatidylinositol phospholipase C activity
B0006629biological_processlipid metabolic process
B0007165biological_processsignal transduction
B0008081molecular_functionphosphoric diester hydrolase activity
B0035556biological_processintracellular signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP A 400
ChainResidue
AGLU49
AVAL182
AARG183
AASN274
ALYS275
AASP277
ALEU278
ACYS330
AALA331
ATHR332
AALF401
ASER50
AMG402
AHOH508
AGLY51
ALYS52
ASER53
ATHR54
ASER156
ALEU180
AARG181

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ALF A 401
ChainResidue
AGLY48
AGLU49
ALYS52
AARG183
APRO185
ATHR186
AVAL206
AGLY208
AGLN209
AGDP400
AMG402
AHOH501
AHOH508

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
ASER53
ATHR186
AGDP400
AALF401
AHOH508

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 900
ChainResidue
BASN333
BGLU362
BASP364
BGLU413

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00270
ChainResidueDetails
BHIS332
ALYS275
AASP277
AALA331
BHIS379
ALYS52
ATHR54
ASER156
ALEU180
AARG181
AARG183
AASN274

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
BPRO573
ATHR186

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BGLU589
BVAL594

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BPHE636
ACYS10

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PDB entries from 2024-10-09

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