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9EJM

Lgl2 bound to the aPKCiota-Par6B complex in its ADP-bound form

Functional Information from GO Data
ChainGOidnamespacecontents
A0001890biological_processplacenta development
A0005096molecular_functionGTPase activator activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005912cellular_componentadherens junction
A0006887biological_processexocytosis
A0006893biological_processGolgi to plasma membrane transport
A0008593biological_processregulation of Notch signaling pathway
A0009791biological_processpost-embryonic development
A0015820biological_processL-leucine transport
A0016332biological_processestablishment or maintenance of polarity of embryonic epithelium
A0030165molecular_functionPDZ domain binding
A0030864cellular_componentcortical actin cytoskeleton
A0030866biological_processcortical actin cytoskeleton organization
A0032878biological_processregulation of establishment or maintenance of cell polarity
A0035264biological_processmulticellular organism growth
A0045159molecular_functionmyosin II binding
A0045197biological_processestablishment or maintenance of epithelial cell apical/basal polarity
A0051294biological_processestablishment of spindle orientation
A0051301biological_processcell division
A0060670biological_processbranching involved in labyrinthine layer morphogenesis
A0060716biological_processlabyrinthine layer blood vessel development
B0000139cellular_componentGolgi membrane
B0000166molecular_functionnucleotide binding
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004697molecular_functiondiacylglycerol-dependent serine/threonine kinase activity
B0004699molecular_functiondiacylglycerol-dependent, calcium-independent serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005543molecular_functionphospholipid binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005768cellular_componentendosome
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005903cellular_componentbrush border
B0005923cellular_componentbicellular tight junction
B0005929cellular_componentcilium
B0006468biological_processprotein phosphorylation
B0006612biological_processprotein targeting to membrane
B0007010biological_processcytoskeleton organization
B0007015biological_processactin filament organization
B0008270molecular_functionzinc ion binding
B0010976biological_processpositive regulation of neuron projection development
B0015630cellular_componentmicrotubule cytoskeleton
B0016020cellular_componentmembrane
B0016192biological_processvesicle-mediated transport
B0016301molecular_functionkinase activity
B0016324cellular_componentapical plasma membrane
B0016477biological_processcell migration
B0016740molecular_functiontransferase activity
B0030010biological_processestablishment of cell polarity
B0031252cellular_componentcell leading edge
B0032869biological_processcellular response to insulin stimulus
B0034351biological_processnegative regulation of glial cell apoptotic process
B0035089biological_processestablishment of apical/basal cell polarity
B0035556biological_processintracellular signal transduction
B0042462biological_processeye photoreceptor cell development
B0043066biological_processnegative regulation of apoptotic process
B0043220cellular_componentSchmidt-Lanterman incisure
B0043434biological_processresponse to peptide hormone
B0043524biological_processnegative regulation of neuron apoptotic process
B0045171cellular_componentintercellular bridge
B0045177cellular_componentapical part of cell
B0045197biological_processestablishment or maintenance of epithelial cell apical/basal polarity
B0045216biological_processcell-cell junction organization
B0045747biological_processpositive regulation of Notch signaling pathway
B0046326biological_processpositive regulation of D-glucose import
B0046872molecular_functionmetal ion binding
B0046903biological_processsecretion
B0048194biological_processGolgi vesicle budding
B0051092biological_processpositive regulation of NF-kappaB transcription factor activity
B0060252biological_processpositive regulation of glial cell proliferation
B0061024biological_processmembrane organization
B0062197biological_processcellular response to chemical stress
B0070062cellular_componentextracellular exosome
B0070160cellular_componenttight junction
B0070555biological_processresponse to interleukin-1
B0072659biological_processprotein localization to plasma membrane
B0098685cellular_componentSchaffer collateral - CA1 synapse
B0098978cellular_componentglutamatergic synapse
B0099072biological_processregulation of postsynaptic membrane neurotransmitter receptor levels
B0106310molecular_functionprotein serine kinase activity
B0120157cellular_componentPAR polarity complex
B1903078biological_processpositive regulation of protein localization to plasma membrane
B2000353biological_processpositive regulation of endothelial cell apoptotic process
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGSYAKVLlVrlkktdriyamk......VVKK
ChainResidueDetails
BILE260-LYS287

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKldNVLL
ChainResidueDetails
BILE374-LEU386

site_idPS00479
Number of Residues50
DetailsZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HtFqakrfnrrah.CaiCtdrIwglgrqgyk.CinCkllvHkkChklvtie..C
ChainResidueDetails
BHIS141-CYS190

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLTGheDgTVRFWDA
ChainResidueDetails
ALEU438-ALA452

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues33
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues41
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues37
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues34
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues42
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues34
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues76
DetailsRepeat: {"description":"WD 8"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues75
DetailsRepeat: {"description":"WD 9"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues61
DetailsRepeat: {"description":"WD 10"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues56
DetailsRepeat: {"description":"WD 11"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues52
DetailsRepeat: {"description":"WD 12"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues53
DetailsRepeat: {"description":"WD 13"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues23
DetailsRepeat: {"description":"WD 14"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"12725730","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"11713277","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11891849","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"11713277","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"16125198","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 756
ChainResidueDetails
BASP378proton shuttle (general acid/base)
BLYS380electrostatic stabiliser
BASN383electrostatic stabiliser

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PDB entries from 2025-10-22

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