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8VSU

Cryo-EM structure of LKB1-STRADalpha-MO25alpha heterocomplex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007165biological_processsignal transduction
A0014823biological_processresponse to activity
A0019900molecular_functionkinase binding
A0030018cellular_componentZ disc
A0030295molecular_functionprotein kinase activator activity
A0032991cellular_componentprotein-containing complex
A0034774cellular_componentsecretory granule lumen
A0035556biological_processintracellular signal transduction
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0070062cellular_componentextracellular exosome
A0071476biological_processcellular hypotonic response
A0097066biological_processresponse to thyroid hormone
A0120283molecular_functionprotein serine/threonine kinase binding
A1901380biological_processnegative regulation of potassium ion transmembrane transport
A1902554cellular_componentserine/threonine protein kinase complex
A1904813cellular_componentficolin-1-rich granule lumen
B0000166molecular_functionnucleotide binding
B0004672molecular_functionprotein kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006468biological_processprotein phosphorylation
B0006611biological_processprotein export from nucleus
B0019900molecular_functionkinase binding
B0030295molecular_functionprotein kinase activator activity
B0032147biological_processactivation of protein kinase activity
B0032991cellular_componentprotein-containing complex
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0070314biological_processG1 to G0 transition
B0140535cellular_componentintracellular protein-containing complex
B1902554cellular_componentserine/threonine protein kinase complex
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0001558biological_processregulation of cell growth
C0001944biological_processvasculature development
C0002039molecular_functionp53 binding
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0006468biological_processprotein phosphorylation
C0006470biological_processprotein dephosphorylation
C0006914biological_processautophagy
C0006915biological_processapoptotic process
C0006974biological_processDNA damage response
C0007165biological_processsignal transduction
C0007283biological_processspermatogenesis
C0007409biological_processaxonogenesis
C0008285biological_processnegative regulation of cell population proliferation
C0010212biological_processresponse to ionizing radiation
C0010508biological_processpositive regulation of autophagy
C0016020cellular_componentmembrane
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0018107biological_processpeptidyl-threonine phosphorylation
C0030010biological_processestablishment of cell polarity
C0030111biological_processregulation of Wnt signaling pathway
C0030154biological_processcell differentiation
C0030275molecular_functionLRR domain binding
C0030295molecular_functionprotein kinase activator activity
C0030308biological_processnegative regulation of cell growth
C0030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
C0032147biological_processactivation of protein kinase activity
C0042593biological_processglucose homeostasis
C0043276biological_processanoikis
C0046777biological_processprotein autophosphorylation
C0046872molecular_functionmetal ion binding
C0051726biological_processregulation of cell cycle
C0070062cellular_componentextracellular exosome
C0070314biological_processG1 to G0 transition
C0071493biological_processcellular response to UV-B
C0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
C0090090biological_processnegative regulation of canonical Wnt signaling pathway
C0106310molecular_functionprotein serine kinase activity
C0120163biological_processnegative regulation of cold-induced thermogenesis
C0140535cellular_componentintracellular protein-containing complex
C1901610biological_processpositive regulation of vesicle transport along microtubule
C1901796biological_processregulation of signal transduction by p53 class mediator
C1904262biological_processnegative regulation of TORC1 signaling
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSYGKVKeVldsetlcr..........RAVK
ChainResidueDetails
CLEU55-LYS78

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHkDIKpgNLLL
ChainResidueDetails
CILE172-LEU184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues260
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues45
DetailsRegion: {"description":"Sufficient for interaction with SIRT1","evidences":[{"source":"PubMed","id":"18687677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues19
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsCompositional bias: {"description":"Pro residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18687677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"11430832","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WTK7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"12805220","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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