5KQ5

AMPK bound to allosteric 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	0004672	molecular_function	protein kinase activity
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	0006633	biological_process	fatty acid biosynthetic process
C	0010628	biological_process	positive regulation of gene expression
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	0043531	molecular_function	ADP binding
C	0044877	molecular_function	protein-containing complex binding
C	0051170	biological_process	import into nucleus

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue STU A 601

Chain	Residue
A	LEU22
A	TYR95
A	VAL96
A	GLY99
A	GLU100
A	GLU143
A	ASN144
A	LEU146
A	ALA156
A	ASP157
A	GLY23
A	VAL24
A	GLY25
A	VAL30
A	ALA43
A	ILE77
A	MET93
A	GLU94

---

site_id	AC2
Number of Residues	10
Details	binding site for residue 6VT A 602

Chain	Residue
A	LEU18
A	GLY19
A	LYS29
A	LYS31
A	ILE46
A	ASP88
B	ARG83
B	THR106
B	ASP108
B	VAL113

---

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 605

Chain	Residue
A	VAL24

---

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

Chain	Residue
A	LYS34
A	LYS41

---

site_id	AC6
Number of Residues	13
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	HIS297
C	ARG298
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	LEU276
C	VAL296
C	HIS297
C	ARG298
C	SO4404

---

site_id	AC8
Number of Residues	13
Details	binding site for residue ADP C 403

Chain	Residue
C	ARG69
C	MET84
C	THR86
C	ILE87
C	THR88
C	ASP89
C	TYR120
C	PRO127
C	LEU128
C	VAL129
C	HIS150
C	ARG151
C	PRO153

---

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

Chain	Residue
C	ARG151
C	THR167
C	AMP402

---

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	8
Details	BINDING: BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92

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:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L

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

---

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

Chain	Residue	Details
C	SER260
A	THR344
A	THR371

---

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

Chain	Residue	Details
C	THR262

---

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

Chain	Residue	Details
C	SER269

---

site_id	SWS_FT_FI6
Number of Residues	5
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q13131

Chain	Residue	Details
A	SER345
A	SER456
A	LYS544

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634

Chain	Residue	Details
A	SER349

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634

Chain	Residue	Details
A	THR357
A	SER524

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:21460634

Chain	Residue	Details
A	SER386

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634, ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	GLY522

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	PRO526

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:12764152, ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	THR532

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