2QRD

Crystal Structure of the Adenylate Sensor from AMP-activated Protein Kinase in complex with ADP and ATP

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	18
Details	BINDING SITE FOR RESIDUE ADP G 1003

Chain	Residue
B	ASP250
G	THR162
G	ARG165
G	ARG287
G	HIS289
G	HOH1503
G	HOH1538
G	HOH1540
G	HOH1547
G	HOH1630
B	GLN251
B	SER252
G	ARG33
G	ILE35
G	ILE55
G	SER57
G	PRO59
G	ARG142

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP G 1001

Chain	Residue
G	ARG141
G	THR191
G	LEU195
G	ALA196
G	ILE216
G	SER217
G	ALA218
G	PRO220
G	ARG290
G	ILE303
G	SER305
G	ALA307
G	ASP308
G	HOH1617

---

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ATP G 1501

Chain	Residue
G	ARG141
G	GLN163
G	THR191
G	LEU195
G	ALA196
G	ASN215
G	ILE216
G	SER217
G	PRO220
G	HIS289
G	ARG290
G	ILE303
G	SER305
G	LEU306
G	ALA307
G	ASP308

---

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADP E 1004

Chain	Residue
D	ASP250
D	GLN251
D	SER252
E	ARG33
E	LEU34
E	ILE35
E	ILE55
E	SER57
E	PRO59
E	ARG142
E	THR162
E	ARG165
E	ARG287
E	HIS289
E	HOH1508
E	HOH1548
E	HOH1551
E	HOH1594

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP E 1002

Chain	Residue
E	ARG139
E	ARG141
E	THR191
E	LEU195
E	ALA196
E	ILE216
E	SER217
E	ALA218
E	PRO220
E	ARG290
E	ILE303
E	SER305
E	ALA307
E	ASP308

---

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ATP E 1502

Chain	Residue
E	ARG139
E	ARG141
E	GLN163
E	THR191
E	ALA196
E	ASN215
E	ILE216
E	SER217
E	PRO220
E	HIS289
E	ARG290
E	ILE303
E	SER305
E	LEU306
E	ALA307
E	ASP308
E	HOH1575

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1

Chain	Residue	Details
G	ILE35
G	ARG142
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

---