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2WTK

Structure of the heterotrimeric LKB1-STRADalpha-MO25alpha complex

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
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0043539molecular_functionprotein serine/threonine kinase activator activity
C0001558biological_processregulation of cell growth
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
C0030010biological_processestablishment of cell polarity
C0030295molecular_functionprotein kinase activator activity
C0042593biological_processglucose homeostasis
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0007165biological_processsignal transduction
D0014823biological_processresponse to activity
D0019900molecular_functionkinase binding
D0030018cellular_componentZ disc
D0030295molecular_functionprotein kinase activator activity
D0032991cellular_componentprotein-containing complex
D0034774cellular_componentsecretory granule lumen
D0035556biological_processintracellular signal transduction
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0070062cellular_componentextracellular exosome
D0071476biological_processcellular hypotonic response
D0097066biological_processresponse to thyroid hormone
D0120283molecular_functionprotein serine/threonine kinase binding
D1901380biological_processnegative regulation of potassium ion transmembrane transport
D1902554cellular_componentserine/threonine protein kinase complex
D1904813cellular_componentficolin-1-rich granule lumen
E0004672molecular_functionprotein kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
E0043539molecular_functionprotein serine/threonine kinase activator activity
F0001558biological_processregulation of cell growth
F0004672molecular_functionprotein kinase activity
F0004674molecular_functionprotein serine/threonine kinase activity
F0005524molecular_functionATP binding
F0006468biological_processprotein phosphorylation
F0030010biological_processestablishment of cell polarity
F0030295molecular_functionprotein kinase activator activity
F0042593biological_processglucose homeostasis
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP B 432
ChainResidue
BILE75
BTHR147
BSER148
BMET150
BSER154
BASP157
BLYS197
BSER199
BHIS200
BARG215
BLYS239
BGLY76
BLYS77
BGLY78
BPHE79
BMET83
BVAL85
BTHR98
BARG100

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ANP C 2
ChainResidue
CGLY56
CGLY58
CSER59
CTYR60
CGLY61
CVAL63
CALA76
CLYS78
CMET129
CGLU130
CCYS132
CGLU138
CLEU183

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 342
ChainResidue
DARG152
DARG194
FLYS108

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ANP E 432
ChainResidue
EILE75
EGLY76
ELYS77
EGLY78
EPHE79
EMET83
EVAL85
ETHR98
EARG100
ETHR147
ESER148
EMET150
ESER154
EASP157
ELYS197
ESER199
EHIS200
EARG215
ELYS239
EPHE415

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ANP F 4
ChainResidue
FGLY56
FGLY58
FSER59
FTYR60
FGLY61
FALA76
FLYS78
FMET129
FGLU130
FCYS132
FGLU138
FLEU183

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 Residues1
DetailsModified residue: {"description":"Phosphothreonine; by LKB1","evidences":[{"source":"PubMed","id":"12805220","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18687677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"11430832","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WTK7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"12805220","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues45
DetailsRegion: {"description":"Sufficient for interaction with SIRT1","evidences":[{"source":"PubMed","id":"18687677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CGLY180
CASP176

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FASN181
FLYS178
FASP176

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FGLY180
FASP176

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS178
CASP176

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FLYS178
FASP176

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BSER195
BLYS197

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ESER195
ELYS197

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CSER216
CLYS178
CASP176

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FSER216
FLYS178
FASP176

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASN181
CLYS178
CASP176

239149

PDB entries from 2025-07-23

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