6C9F

AMP-activated protein kinase bound to pharmacological activator R734

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	0004672	molecular_function	protein kinase activity
C	0004691	molecular_function	cAMP-dependent protein kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006110	biological_process	regulation of glycolytic process
C	0006468	biological_process	protein phosphorylation
C	0006633	biological_process	fatty acid biosynthetic process
C	0007165	biological_process	signal transduction
C	0007283	biological_process	spermatogenesis
C	0008603	molecular_function	cAMP-dependent protein kinase regulator activity
C	0010628	biological_process	positive regulation of gene expression
C	0016020	cellular_component	membrane
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	0043531	molecular_function	ADP binding
C	0045860	biological_process	positive regulation of protein kinase activity
C	0051170	biological_process	import into nucleus

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue R34 A 601

Chain	Residue
A	VAL13
A	ASP90
A	PHE92
B	ARG83
B	ASP108
B	VAL113
A	LEU20
A	PHE29
A	GLY30
A	LYS31
A	LYS33
A	ILE48
A	ASN50
A	LYS53

---

site_id	AC2
Number of Residues	14
Details	binding site for residue STU A 602

Chain	Residue
A	GLY25
A	VAL26
A	ALA45
A	MET95
A	GLU96
A	TYR97
A	VAL98
A	GLY101
A	GLU102
A	GLU145
A	ASN146
A	LEU148
A	ALA158
A	ASP159

---

site_id	AC3
Number of Residues	11
Details	binding site for residue AMP C 1101

Chain	Residue
C	MET84
C	THR86
C	THR88
C	ASP89
C	PRO127
C	LEU128
C	VAL129
C	ILE149
C	HIS150
C	ARG151
C	PRO153

---

site_id	AC4
Number of Residues	12
Details	binding site for residue AMP C 1102

Chain	Residue
C	ARG69
C	ILE239
C	SER241
C	PHE243
C	ASP244
C	ARG268
C	GLY274
C	VAL275
C	LEU276
C	VAL296
C	HIS297
C	ARG298

---

site_id	AC5
Number of Residues	13
Details	binding site for residue AMP C 1103

Chain	Residue
C	HIS150
C	THR199
C	ILE203
C	ALA204
C	VAL224
C	SER225
C	ALA226
C	PRO228
C	ARG298
C	ILE311
C	SER313
C	SER315
C	ASP316

---

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	LEU24-LYS47

---

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

Chain	Residue	Details
A	VAL137-LEU149

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P80385

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

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF

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

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385

Chain	Residue	Details
C	SER260
C	SER269

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P80385

Chain	Residue	Details
C	THR262

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9R078

Chain	Residue	Details
B	SER182
A	HIS533

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR346

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER347

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P54645

Chain	Residue	Details
A	SER351

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P54645

Chain	Residue	Details
A	THR359

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR373

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P54645

Chain	Residue	Details
A	SER388

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER458

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	GLY531

---

site_id	SWS_FT_FI14
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	ILE535

---

site_id	SWS_FT_FI15
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	CYS541

---

site_id	SWS_FT_FI16
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain

Residue

Details

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