Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7LZ4

Crystal structure of A211D mutant of Protein Kinase A RIa subunit, a Carney Complex mutation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001932	biological_process	regulation of protein phosphorylation
A	0005952	cellular_component	cAMP-dependent protein kinase complex
A	0008603	molecular_function	cAMP-dependent protein kinase regulator activity
B	0001932	biological_process	regulation of protein phosphorylation
B	0005952	cellular_component	cAMP-dependent protein kinase complex
B	0008603	molecular_function	cAMP-dependent protein kinase regulator activity
C	0001932	biological_process	regulation of protein phosphorylation
C	0005952	cellular_component	cAMP-dependent protein kinase complex
C	0008603	molecular_function	cAMP-dependent protein kinase regulator activity
D	0001932	biological_process	regulation of protein phosphorylation
D	0005952	cellular_component	cAMP-dependent protein kinase complex
D	0008603	molecular_function	cAMP-dependent protein kinase regulator activity
E	0001932	biological_process	regulation of protein phosphorylation
E	0005952	cellular_component	cAMP-dependent protein kinase complex
E	0008603	molecular_function	cAMP-dependent protein kinase regulator activity
F	0001932	biological_process	regulation of protein phosphorylation
F	0005952	cellular_component	cAMP-dependent protein kinase complex
F	0008603	molecular_function	cAMP-dependent protein kinase regulator activity
G	0001932	biological_process	regulation of protein phosphorylation
G	0005952	cellular_component	cAMP-dependent protein kinase complex
G	0008603	molecular_function	cAMP-dependent protein kinase regulator activity
H	0001932	biological_process	regulation of protein phosphorylation
H	0005952	cellular_component	cAMP-dependent protein kinase complex
H	0008603	molecular_function	cAMP-dependent protein kinase regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue CMP A 401

Chain	Residue
A	PHE198
A	GLY199
A	GLU200
A	LEU201
A	ALA202
A	ARG209
A	ALA210
A	ASP211
A	TRP260

site_id	AC2
Number of Residues	13
Details	binding site for residue CMP A 402

Chain	Residue
A	VAL300
A	GLN302
A	VAL313
A	PHE322
A	GLY323
A	GLU324
A	ILE325
A	ARG333
A	ALA334
A	ALA335
A	TYR371
A	ASN372
A	SER373

site_id	AC3
Number of Residues	9
Details	binding site for residue CMP B 401

Chain	Residue
B	PHE198
B	GLY199
B	GLU200
B	LEU201
B	ALA202
B	ARG209
B	ALA210
B	ASP211
B	TRP260

site_id	AC4
Number of Residues	13
Details	binding site for residue CMP B 402

Chain	Residue
B	VAL300
B	GLN302
B	VAL313
B	GLY323
B	GLU324
B	ILE325
B	ALA326
B	PRO332
B	ARG333
B	ALA334
B	ALA335
B	TYR371
B	ASN372

site_id	AC5
Number of Residues	9
Details	binding site for residue CMP C 401

Chain	Residue
C	PHE198
C	GLY199
C	GLU200
C	LEU201
C	ALA202
C	ARG209
C	ALA210
C	ASP211
C	TRP260

site_id	AC6
Number of Residues	14
Details	binding site for residue CMP C 402

Chain	Residue
C	VAL281
C	VAL300
C	VAL313
C	PHE322
C	GLY323
C	GLU324
C	ILE325
C	ALA326
C	ARG333
C	ALA334
C	ALA335
C	TYR371
C	ASN372
C	SER373

site_id	AC7
Number of Residues	9
Details	binding site for residue CMP D 401

Chain	Residue
D	PHE198
D	GLY199
D	GLU200
D	LEU201
D	ALA202
D	ARG209
D	ALA210
D	ASP211
D	TRP260

site_id	AC8
Number of Residues	14
Details	binding site for residue CMP D 402

Chain	Residue
D	GLN302
D	VAL313
D	PHE322
D	GLY323
D	GLU324
D	ILE325
D	ALA326
D	PRO332
D	ARG333
D	ALA334
D	ALA335
D	TYR371
D	ASN372
D	SER373

site_id	AC9
Number of Residues	9
Details	binding site for residue CMP E 401

Chain	Residue
E	PHE198
E	GLY199
E	GLU200
E	LEU201
E	ALA202
E	ARG209
E	ALA210
E	ASP211
E	TRP260

site_id	AD1
Number of Residues	13
Details	binding site for residue CMP E 402

Chain	Residue
E	VAL300
E	VAL313
E	PHE322
E	GLY323
E	GLU324
E	ILE325
E	ALA326
E	ARG333
E	ALA334
E	ALA335
E	VAL337
E	TYR371
E	ASN372

site_id	AD2
Number of Residues	9
Details	binding site for residue CMP F 401

Chain	Residue
F	PHE198
F	GLY199
F	GLU200
F	LEU201
F	ALA202
F	ARG209
F	ALA210
F	ASP211
F	TRP260

site_id	AD3
Number of Residues	14
Details	binding site for residue CMP F 402

Chain	Residue
F	VAL300
F	GLN302
F	VAL313
F	PHE322
F	GLY323
F	GLU324
F	ILE325
F	ALA326
F	ARG333
F	ALA334
F	ALA335
F	VAL337
F	TYR371
F	ASN372

site_id	AD4
Number of Residues	10
Details	binding site for residue CMP G 401

Chain	Residue
G	PHE198
G	GLY199
G	GLU200
G	LEU201
G	ALA202
G	ARG209
G	ALA210
G	ASP211
G	LYS259
G	TRP260

site_id	AD5
Number of Residues	11
Details	binding site for residue CMP G 402

Chain	Residue
G	VAL313
G	PHE322
G	GLY323
G	GLU324
G	ALA326
G	ARG333
G	ALA334
G	ALA335
G	TYR371
G	ASN372
G	SER373

site_id	AD6
Number of Residues	10
Details	binding site for residue CMP H 401

Chain	Residue
H	PHE198
H	GLY199
H	GLU200
H	LEU201
H	ALA202
H	ARG209
H	ALA210
H	ASP211
H	LYS259
H	TRP260

site_id	AD7
Number of Residues	14
Details	binding site for residue CMP H 402

Chain	Residue
H	VAL281
H	VAL300
H	VAL313
H	PHE322
H	GLY323
H	GLU324
H	ILE325
H	ALA326
H	ARG333
H	ALA334
H	ALA335
H	VAL337
H	TYR371
H	ASN372

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL162-GLY178
A	ILE280-GLY296

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

Chain	Residue	Details
A	PHE322-ALA339

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	BINDING:

Chain	Residue	Details
B	ARG209
B	ILE253
B	GLU324
B	ARG333
C	LEU135
C	GLU200
C	ARG209
C	ILE253
C	GLU324
C	ARG333
D	LEU135
D	GLU200
D	ARG209
D	ILE253
D	GLU324
D	ARG333
E	LEU135
E	GLU200
E	ARG209
E	ILE253
E	GLU324
E	ARG333
F	LEU135
F	GLU200
F	ARG209
F	ILE253
F	GLU324
F	ARG333
G	LEU135
G	GLU200
G	ARG209
G	ILE253
G	GLU324
G	ARG333
H	LEU135
H	GLU200
H	ARG209
H	ILE253
H	GLU324
H	ARG333
A	LEU135
A	GLU200
A	ARG209
A	ILE253
A	GLU324
A	ARG333
B	LEU135
B	GLU200

site_id	SWS_FT_FI2
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P09456

Chain	Residue	Details
C	SER256
D	SER256
E	SER256
F	SER256
G	SER256
H	SER256
A	SER256
B	SER256

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)