Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WTK

Structure of the heterotrimeric LKB1-STRADalpha-MO25alpha complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0007165	biological_process	signal transduction
A	0010800	biological_process	positive regulation of peptidyl-threonine phosphorylation
A	0014823	biological_process	response to activity
A	0018105	biological_process	peptidyl-serine phosphorylation
A	0019900	molecular_function	kinase binding
A	0030018	cellular_component	Z disc
A	0030295	molecular_function	protein kinase activator activity
A	0032991	cellular_component	protein-containing complex
A	0034774	cellular_component	secretory granule lumen
A	0035556	biological_process	intracellular signal transduction
A	0043539	molecular_function	protein serine/threonine kinase activator activity
A	0070062	cellular_component	extracellular exosome
A	0071476	biological_process	cellular hypotonic response
A	0071902	biological_process	positive regulation of protein serine/threonine kinase activity
A	0097066	biological_process	response to thyroid hormone
A	1901017	biological_process	negative regulation of potassium ion transmembrane transporter activity
A	1901380	biological_process	negative regulation of potassium ion transmembrane transport
A	1902554	cellular_component	serine/threonine protein kinase complex
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
B	0043539	molecular_function	protein serine/threonine kinase activator activity
C	0001558	biological_process	regulation of cell growth
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
C	0030010	biological_process	establishment of cell polarity
C	0030295	molecular_function	protein kinase activator activity
C	0042593	biological_process	glucose homeostasis
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0007165	biological_process	signal transduction
D	0010800	biological_process	positive regulation of peptidyl-threonine phosphorylation
D	0014823	biological_process	response to activity
D	0018105	biological_process	peptidyl-serine phosphorylation
D	0019900	molecular_function	kinase binding
D	0030018	cellular_component	Z disc
D	0030295	molecular_function	protein kinase activator activity
D	0032991	cellular_component	protein-containing complex
D	0034774	cellular_component	secretory granule lumen
D	0035556	biological_process	intracellular signal transduction
D	0043539	molecular_function	protein serine/threonine kinase activator activity
D	0070062	cellular_component	extracellular exosome
D	0071476	biological_process	cellular hypotonic response
D	0071902	biological_process	positive regulation of protein serine/threonine kinase activity
D	0097066	biological_process	response to thyroid hormone
D	1901017	biological_process	negative regulation of potassium ion transmembrane transporter activity
D	1901380	biological_process	negative regulation of potassium ion transmembrane transport
D	1902554	cellular_component	serine/threonine protein kinase complex
D	1904813	cellular_component	ficolin-1-rich granule lumen
E	0004672	molecular_function	protein kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
E	0043539	molecular_function	protein serine/threonine kinase activator activity
F	0001558	biological_process	regulation of cell growth
F	0004672	molecular_function	protein kinase activity
F	0004674	molecular_function	protein serine/threonine kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
F	0030010	biological_process	establishment of cell polarity
F	0030295	molecular_function	protein kinase activator activity
F	0042593	biological_process	glucose homeostasis

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ANP B 432

Chain	Residue
B	ILE75
B	THR147
B	SER148
B	MET150
B	SER154
B	ASP157
B	LYS197
B	SER199
B	HIS200
B	ARG215
B	LYS239
B	GLY76
B	LYS77
B	GLY78
B	PHE79
B	MET83
B	VAL85
B	THR98
B	ARG100

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ANP C 2

Chain	Residue
C	GLY56
C	GLY58
C	SER59
C	TYR60
C	GLY61
C	VAL63
C	ALA76
C	LYS78
C	MET129
C	GLU130
C	CYS132
C	GLU138
C	LEU183

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 342

Chain	Residue
D	ARG152
D	ARG194
F	LYS108

site_id	AC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ANP E 432

Chain	Residue
E	ILE75
E	GLY76
E	LYS77
E	GLY78
E	PHE79
E	MET83
E	VAL85
E	THR98
E	ARG100
E	THR147
E	SER148
E	MET150
E	SER154
E	ASP157
E	LYS197
E	SER199
E	HIS200
E	ARG215
E	LYS239
E	PHE415

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP F 4

Chain	Residue
F	GLY56
F	GLY58
F	SER59
F	TYR60
F	GLY61
F	ALA76
F	LYS78
F	MET129
F	GLU130
F	CYS132
F	GLU138
F	LEU183

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSYGKVKeVldsetlcr..........RAVK

Chain	Residue	Details
C	LEU55-LYS78

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHkDIKpgNLLL

Chain	Residue	Details
C	ILE172-LEU184

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
C	ASP176
F	ASP176
E	THR329
E	THR419

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
C	LEU55
F	LEU55

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
C	LYS78
F	LYS78

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18687677

Chain	Residue	Details
C	LYS44
F	LYS97
F	LYS296
F	LYS311
C	LYS48
C	LYS96
C	LYS97
C	LYS296
C	LYS311
F	LYS44
F	LYS48
F	LYS96

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269\|PubMed:11430832

Chain	Residue	Details
C	THR189
F	THR189

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q9WTK7

Chain	Residue	Details
C	SER325
F	SER325

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269\|PubMed:12805220

Chain	Residue	Details
C	THR336
F	THR336

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	GLY180
C	ASP176

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	ASN181
F	LYS178
F	ASP176

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	GLY180
F	ASP176

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	LYS178
C	ASP176

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	LYS178
F	ASP176

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	SER195
B	LYS197

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	SER195
E	LYS197

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	SER216
C	LYS178
C	ASP176

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	SER216
F	LYS178
F	ASP176

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASN181
C	LYS178
C	ASP176

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)