2OOX

Crystal structure of the adenylate sensor from AMP-activated protein kinase complexed with AMP

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0006357	biological_process	regulation of transcription by RNA polymerase II
E	0007165	biological_process	signal transduction
E	0010514	biological_process	induction of conjugation with cellular fusion
E	0016208	molecular_function	AMP binding
E	0019887	molecular_function	protein kinase regulator activity
E	0019901	molecular_function	protein kinase binding
E	0030295	molecular_function	protein kinase activator activity
E	0031588	cellular_component	nucleotide-activated protein kinase complex
E	0043531	molecular_function	ADP binding
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006357	biological_process	regulation of transcription by RNA polymerase II
G	0007165	biological_process	signal transduction
G	0010514	biological_process	induction of conjugation with cellular fusion
G	0016208	molecular_function	AMP binding
G	0019887	molecular_function	protein kinase regulator activity
G	0019901	molecular_function	protein kinase binding
G	0030295	molecular_function	protein kinase activator activity
G	0031588	cellular_component	nucleotide-activated protein kinase complex
G	0043531	molecular_function	ADP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AMP E 401

Chain	Residue
E	ARG141
E	SER305
E	ASP308
E	HOH433
E	THR191
E	LEU195
E	ALA196
E	ILE216
E	SER217
E	PRO220
E	ARG290
E	ILE303

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE AMP G 401

Chain	Residue
B	GLU223
G	ARG139
G	ARG141
G	THR191
G	ALA196
G	ILE216
G	SER217
G	ALA218
G	PRO220
G	ARG290
G	ILE303
G	SER305
G	ASP308
G	HOH468
G	HOH469
G	HOH536
G	HOH538

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0007744|PDB:2QR1, ECO:0007744|PDB:2QRC, ECO:0007744|PDB:2QRD

Chain	Residue	Details
B	ASP250
D	ASP250
G	THR162
G	ARG287
E	ILE35
E	ARG142
E	THR162
E	ARG287

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:17289942, ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2OOY

Chain	Residue	Details
G	ARG141
G	ARG290
E	ARG141
E	ARG290

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOY

Chain	Residue	Details
G	THR191
G	ALA196
G	SER217
G	ILE303
E	THR191
E	ALA196
E	SER217
E	ILE303

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOX

Chain	Residue	Details
G	SER305
E	SER305

---