2V92

Crystal structure of the regulatory fragment of mammalian AMPK in complexes with ATP-AMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004679	molecular_function	AMP-activated protein kinase activity
E	0004672	molecular_function	protein kinase activity
E	0004679	molecular_function	AMP-activated protein kinase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006110	biological_process	regulation of glycolytic process
E	0006633	biological_process	fatty acid biosynthetic process
E	0010628	biological_process	positive regulation of gene expression
E	0016208	molecular_function	AMP binding
E	0019887	molecular_function	protein kinase regulator activity
E	0019901	molecular_function	protein kinase binding
E	0031588	cellular_component	nucleotide-activated protein kinase complex
E	0031669	biological_process	cellular response to nutrient levels
E	0032991	cellular_component	protein-containing complex
E	0042149	biological_process	cellular response to glucose starvation
E	0043531	molecular_function	ADP binding
E	0043609	biological_process	regulation of carbon utilization
E	0044877	molecular_function	protein-containing complex binding
E	0045722	biological_process	positive regulation of gluconeogenesis
E	0051170	biological_process	import into nucleus

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP E1327

Chain	Residue
E	ARG69
E	VAL275
E	LEU276
E	VAL296
E	HIS297
E	ARG298
E	HOH2229
E	HOH2230
E	HOH2231
E	HOH2232
E	HOH2233
E	ARG151
E	HOH2234
E	HOH2235
E	LYS169
E	ILE239
E	SER241
E	PHE243
E	ASP244
E	ARG268
E	GLY274

---

site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP E1328

Chain	Residue
E	ARG69
E	MET84
E	THR86
E	ILE87
E	THR88
E	ASP89
E	PRO127
E	LEU128
E	VAL129
E	ILE149
E	HIS150
E	ARG151
E	PRO153
E	SER225
E	LYS242
E	HOH2036
E	HOH2232
E	HOH2236
E	HOH2237
E	HOH2238

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE AMP E1329

Chain	Residue
A	ARG457
E	HIS150
E	THR199
E	ASN202
E	ILE203
E	ALA204
E	VAL224
E	SER225
E	ALA226
E	HIS297
E	ILE311
E	SER313
E	SER315
E	ASP316
E	HOH2199
E	HOH2239
E	HOH2241
E	HOH2242

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92

Chain	Residue	Details
E	ARG69
E	MET84
E	VAL129
E	ARG151
E	LYS169
E	SER241
E	ARG268
E	LEU276

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L

Chain	Residue	Details
E	HIS150
E	THR199
E	ALA204
E	SER225
E	HIS297
E	SER313

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634

Chain	Residue	Details
E	SER260

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634

Chain	Residue	Details
E	THR262

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:21460634

Chain	Residue	Details
E	SER269

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:12764152, ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	ASP496

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