Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5UFU

Structure of AMPK bound to activator

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004679	molecular_function	AMP-activated protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
C	0000166	molecular_function	nucleotide binding
C	0004679	molecular_function	AMP-activated protein kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006110	biological_process	regulation of glycolytic process
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
C	0016208	molecular_function	AMP binding
C	0019887	molecular_function	protein kinase regulator activity
C	0019901	molecular_function	protein kinase binding
C	0031588	cellular_component	nucleotide-activated protein kinase complex
C	0031669	biological_process	cellular response to nutrient levels
C	0032991	cellular_component	protein-containing complex
C	0042149	biological_process	cellular response to glucose starvation
C	0043531	molecular_function	ADP binding
C	0043609	biological_process	regulation of carbon utilization
C	0044877	molecular_function	protein-containing complex binding
C	0045722	biological_process	positive regulation of gluconeogenesis
C	0051170	biological_process	import into nucleus

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue STU A 601

Chain	Residue
A	LEU22
A	VAL96
A	GLY99
A	GLU100
A	GLU143
A	ASN144
A	LEU146
A	ASP157
A	GLY23
A	VAL24
A	GLY25
A	ALA43
A	ILE77
A	MET93
A	GLU94
A	TYR95

site_id	AC2
Number of Residues	16
Details	binding site for residue 85V A 602

Chain	Residue
A	VAL11
A	LEU18
A	GLY19
A	PHE27
A	LYS29
A	LYS31
A	ILE46
A	ASN48
A	LYS51
A	ASP88
A	ASP217
B	ARG83
B	THR106
B	ASP108
B	VAL113
B	ILE115

site_id	AC3
Number of Residues	2
Details	binding site for residue CL A 603

Chain	Residue
A	SER97
A	ALA149

site_id	AC4
Number of Residues	1
Details	binding site for residue CL A 604

Chain	Residue
A	VAL24

site_id	AC5
Number of Residues	2
Details	binding site for residue SO4 A 606

Chain	Residue
A	LYS34
A	LYS41

site_id	AC6
Number of Residues	11
Details	binding site for residue AMP C 401

Chain	Residue
C	HIS150
C	THR199
C	ILE203
C	ALA204
C	VAL224
C	SER225
C	ALA226
C	ILE311
C	SER313
C	SER315
C	ASP316

site_id	AC7
Number of Residues	11
Details	binding site for residue AMP C 402

Chain	Residue
C	ARG69
C	ILE239
C	SER241
C	PHE243
C	ASP244
C	ARG268
C	GLY274
C	LEU276
C	VAL296
C	HIS297
C	ARG298

site_id	AC8
Number of Residues	12
Details	binding site for residue ADP C 403

Chain	Residue
C	ARG69
C	MET84
C	THR86
C	THR88
C	ASP89
C	TYR120
C	PRO127
C	LEU128
C	VAL129
C	ILE149
C	HIS150
C	ARG151

site_id	AC9
Number of Residues	3
Details	binding site for residue SO4 C 404

Chain	Residue
C	ARG151
C	THR167
C	HIS297

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU22-LYS45

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

Chain	Residue	Details
A	VAL135-LEU147

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q13131","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by LKB1 and CaMKK2","evidences":[{"source":"PubMed","id":"15980064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16054095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16308421","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"12764152","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q13131","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"UniProtKB","id":"P54645","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"12764152","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"11171104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12764152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9305909","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9Y478","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9R078","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	60
Details	Domain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	62
Details	Domain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	21
Details	Motif: {"description":"AMPK pseudosubstrate"}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V92","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21399626","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V8Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y8L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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