4EAG

Co-crystal structure of an chimeric AMPK core with ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
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	17
Details	BINDING SITE FOR RESIDUE ATP C 401

Chain	Residue
C	MET84
C	ILE149
C	HIS150
C	ARG151
C	PRO153
C	SER225
C	PHE243
C	HOH509
C	HOH539
C	THR86
C	ILE87
C	THR88
C	ASP89
C	GLN122
C	PRO127
C	LEU128
C	VAL129

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP C 402

Chain	Residue
C	HIS150
C	THR199
C	ALA204
C	VAL224
C	SER225
C	ALA226
C	PRO228
C	HIS297
C	ARG298
C	SER313
C	LEU314
C	SER315
C	ASP316
C	HOH515
C	HOH538

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TAM C 403

Chain	Residue
C	VAL68
C	ARG69
C	ARG151
C	THR167
C	LYS169
C	ARG170
C	HIS297
C	HOH503
C	HOH521
C	HOH527
C	HOH536

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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_FI2
Number of Residues	62
Details	Domain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	21
Details	Motif: {"description":"AMPK pseudosubstrate"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
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_FI5
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_FI6
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_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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