4Z07

Co-crystal structure of the tandem CNB (CNB-A/B) domains of human PKG I beta with cGMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001932	biological_process	regulation of protein phosphorylation
A	0004692	molecular_function	cGMP-dependent protein kinase activity
A	0005524	molecular_function	ATP binding
A	0005952	cellular_component	cAMP-dependent protein kinase complex
A	0008603	molecular_function	cAMP-dependent protein kinase regulator activity
C	0001932	biological_process	regulation of protein phosphorylation
C	0004692	molecular_function	cGMP-dependent protein kinase activity
C	0005524	molecular_function	ATP binding
C	0005952	cellular_component	cAMP-dependent protein kinase complex
C	0008603	molecular_function	cAMP-dependent protein kinase regulator activity
E	0001932	biological_process	regulation of protein phosphorylation
E	0004692	molecular_function	cGMP-dependent protein kinase activity
E	0005524	molecular_function	ATP binding
E	0005952	cellular_component	cAMP-dependent protein kinase complex
E	0008603	molecular_function	cAMP-dependent protein kinase regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue PCG A 401

Chain	Residue
A	LEU172
A	ALA194
A	HOH520
C	GLU229
C	HOH506
A	CYS173
A	PHE181
A	GLY182
A	GLU183
A	LEU184
A	ALA185
A	ARG192
A	THR193

---

site_id	AC2
Number of Residues	16
Details	binding site for residue PCG A 402

Chain	Residue
A	VAL283
A	ARG285
A	LEU296
A	ARG297
A	PHE305
A	GLY306
A	GLU307
A	LYS308
A	ALA309
A	GLU313
A	ARG316
A	THR317
A	ALA318
A	VAL320
A	TYR351
A	HOH552

---

site_id	AC3
Number of Residues	14
Details	binding site for residue PCG C 401

Chain	Residue
A	GLU229
C	VAL165
C	LEU172
C	PHE181
C	GLY182
C	GLU183
C	LEU184
C	ALA185
C	ARG192
C	THR193
C	ALA194
C	HOH502
C	HOH508
C	HOH518

---

site_id	AC4
Number of Residues	13
Details	binding site for residue PCG C 402

Chain	Residue
C	ILE264
C	LEU296
C	ARG297
C	PHE305
C	GLY306
C	GLU307
C	LYS308
C	ALA309
C	ARG316
C	THR317
C	ALA318
C	VAL320
C	TYR351

---

site_id	AC5
Number of Residues	4
Details	binding site for residue SO4 C 403

Chain	Residue
C	VAL151
C	SER153
C	LEU154
C	ARG192

---

site_id	AC6
Number of Residues	5
Details	binding site for residue IPA C 404

Chain	Residue
C	PHE98
C	PHE98
C	TYR99
C	CYS133
C	TYR135

---

site_id	AC7
Number of Residues	4
Details	binding site for residue IPA C 405

Chain	Residue
C	ARG265
C	ASP271
C	THR272
C	ARG316

---

site_id	AC8
Number of Residues	15
Details	binding site for residue PCG E 401

Chain	Residue
A	ASN282
A	PHE295
A	THR298
E	ILE146
E	VAL165
E	LEU172
E	CYS173
E	PHE181
E	GLY182
E	GLU183
E	LEU184
E	ALA185
E	ARG192
E	THR193
E	ALA194

---

Functional Information from PROSITE/UniProt

site_id	PS00888
Number of Residues	17
Details	CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. IIkEGDvGSlVYVMedG

Chain	Residue	Details
A	ILE145-GLY161
A	ILE263-GLY279

---

site_id	PS00889
Number of Residues	18
Details	CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGElAIlynct......RTAtVkT

Chain	Residue	Details
A	PHE181-THR198
A	PHE305-ALA322

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	234
Details	Region: {"description":"cGMP-binding, high affinity"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21526164","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OD0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24239458","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25271401","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4KU7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QXK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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