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4QJ5

Structure of a fragment of human phospholipase C-beta3 delta472-581, bound to IP3 and 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
A0005096molecular_functionGTPase activator activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005834cellular_componentheterotrimeric G-protein complex
A0005886cellular_componentplasma membrane
A0005901cellular_componentcaveola
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
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
A0043066biological_processnegative regulation of apoptotic process
A0043267biological_processnegative regulation of potassium ion transport
A0044297cellular_componentcell body
A0044877molecular_functionprotein-containing complex binding
A0045202cellular_componentsynapse
A0045634biological_processregulation of melanocyte differentiation
A0046872molecular_functionmetal ion binding
A0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
A0048066biological_processdevelopmental pigmentation
A0048661biological_processpositive regulation of smooth muscle cell proliferation
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 Residues20
DetailsBINDING SITE FOR RESIDUE GDP A 400
ChainResidue
AGLU49
AARG183
AASN274
ALYS275
AASP277
ALEU278
ACYS330
AALA331
ATHR332
AALF401
AMG402
ASER50
AHOH502
AGLY51
ALYS52
ASER53
ATHR54
ALEU180
AARG181
AVAL182

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
AHOH502

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
ASER53
ATHR186
AGDP400
AALF401
AHOH502

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 901
ChainResidue
BASN333
BGLU362
BASP364
BGLU413
BI3P902

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE I3P B 902
ChainResidue
BHIS332
BASN333
BGLU362
BHIS379
BGLU413
BSER619
BARG646
BTYR648
BCA901

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00270
ChainResidueDetails
BHIS332
BHIS379

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
BPRO573
ALEU180
ATHR186
AASN274
AALA331

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 2024-07-31

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