Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1RDQ

Hydrolysis of ATP in the crystal of Y204A mutant of cAMP-dependent protein kinase

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0000122	biological_process	negative regulation of transcription by RNA polymerase II
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0001669	cellular_component	acrosomal vesicle
E	0001707	biological_process	mesoderm formation
E	0001843	biological_process	neural tube closure
E	0004672	molecular_function	protein kinase activity
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0004691	molecular_function	cAMP-dependent protein kinase activity
E	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005813	cellular_component	centrosome
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0005929	cellular_component	cilium
E	0005930	cellular_component	axoneme
E	0005952	cellular_component	cAMP-dependent protein kinase complex
E	0006397	biological_process	mRNA processing
E	0006468	biological_process	protein phosphorylation
E	0006611	biological_process	protein export from nucleus
E	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
E	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
E	0016020	cellular_component	membrane
E	0016301	molecular_function	kinase activity
E	0016607	cellular_component	nuclear speck
E	0016740	molecular_function	transferase activity
E	0018105	biological_process	peptidyl-serine phosphorylation
E	0019901	molecular_function	protein kinase binding
E	0019904	molecular_function	protein domain specific binding
E	0030007	biological_process	intracellular potassium ion homeostasis
E	0030145	molecular_function	manganese ion binding
E	0031410	cellular_component	cytoplasmic vesicle
E	0031514	cellular_component	motile cilium
E	0031594	cellular_component	neuromuscular junction
E	0031625	molecular_function	ubiquitin protein ligase binding
E	0032024	biological_process	positive regulation of insulin secretion
E	0034237	molecular_function	protein kinase A regulatory subunit binding
E	0034605	biological_process	cellular response to heat
E	0036126	cellular_component	sperm flagellum
E	0042995	cellular_component	cell projection
E	0044853	cellular_component	plasma membrane raft
E	0045542	biological_process	positive regulation of cholesterol biosynthetic process
E	0045667	biological_process	regulation of osteoblast differentiation
E	0045722	biological_process	positive regulation of gluconeogenesis
E	0045879	biological_process	negative regulation of smoothened signaling pathway
E	0046827	biological_process	positive regulation of protein export from nucleus
E	0048240	biological_process	sperm capacitation
E	0048471	cellular_component	perinuclear region of cytoplasm
E	0050766	biological_process	positive regulation of phagocytosis
E	0050804	biological_process	modulation of chemical synaptic transmission
E	0051726	biological_process	regulation of cell cycle
E	0061136	biological_process	regulation of proteasomal protein catabolic process
E	0070417	biological_process	cellular response to cold
E	0070613	biological_process	regulation of protein processing
E	0071333	biological_process	cellular response to glucose stimulus
E	0071374	biological_process	cellular response to parathyroid hormone stimulus
E	0071377	biological_process	cellular response to glucagon stimulus
E	0097546	cellular_component	ciliary base
E	0098794	cellular_component	postsynapse
E	0098978	cellular_component	glutamatergic synapse
E	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
E	0106310	molecular_function	protein serine kinase activity
E	0141156	biological_process	cAMP/PKA signal transduction
E	1904262	biological_process	negative regulation of TORC1 signaling
E	1904539	biological_process	negative regulation of glycolytic process through fructose-6-phosphate
E	1990044	biological_process	protein localization to lipid droplet
E	2000810	biological_process	regulation of bicellular tight junction assembly
I	0004862	molecular_function	cAMP-dependent protein kinase inhibitor activity
I	0006469	biological_process	negative regulation of protein kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PO4 E 598

Chain	Residue
E	SER53
E	MG602
E	HOH1029
E	HOH1146
I	ALA521
E	PHE54
E	ASP166
E	LYS168
E	ASN171
E	ASP184
E	THR201
E	ADP599
E	MG601

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 601

Chain	Residue
E	ASN171
E	ASP184
E	PO4598
E	ADP599
E	ATP600
E	HOH1146

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 602

Chain	Residue
E	ASP184
E	PO4598
E	ADP599
E	ATP600
E	HOH1028
E	HOH1029

site_id	AC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP E 599

Chain	Residue
E	GLY50
E	GLY52
E	SER53
E	PHE54
E	GLY55
E	VAL57
E	ALA70
E	LYS72
E	VAL104
E	MET120
E	GLU121
E	VAL123
E	GLU127
E	GLU170
E	ASN171
E	LEU173
E	THR183
E	ASP184
E	PHE327
E	PO4598
E	MG601
E	MG602
E	HOH1028
E	HOH1035
E	HOH1146
I	ARG518

site_id	AC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE ATP E 600

Chain	Residue
E	GLY50
E	GLY52
E	SER53
E	PHE54
E	GLY55
E	VAL57
E	ALA70
E	LYS72
E	VAL104
E	MET120
E	GLU121
E	VAL123
E	GLU127
E	ASP166
E	LYS168
E	GLU170
E	ASN171
E	LEU173
E	THR183
E	ASP184
E	PHE327
E	MG601
E	MG602
E	HOH1020
E	HOH1028
E	HOH1029
E	HOH1035
E	HOH1146
I	ARG518

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MRD E 800

Chain	Residue
E	VAL15
E	PHE18
E	LEU152
E	GLU155
E	TYR306

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL E 700

Chain	Residue
E	ASP44
E	ARG45
E	PRO141
E	HOH1147
E	HOH1171
E	HOH1275
E	HOH1315
E	HOH1408

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhkesgnh..........YAMK

Chain	Residue	Details
E	LEU49-LYS72

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI

Chain	Residue	Details
E	LEU162-ILE174

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
E	LEU167

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
E	GLY50
E	ILE73
E	TYR122
E	PRO169

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Deamidated asparagine; partial => ECO:0000269\|PubMed:11141074

Chain	Residue	Details
E	ALA3

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269\|PubMed:11141074, ECO:0000269\|PubMed:8395513

Chain	Residue	Details
E	GLU11

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P17612

Chain	Residue	Details
E	LEU49
E	TRP196

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:22323819, ECO:0000305\|PubMed:8395513

Chain	Residue	Details
E	GLU140

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269\|PubMed:22323819, ECO:0000269\|PubMed:8395513, ECO:0000269\|PubMed:9707564

Chain	Residue	Details
E	LEU198

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:21866565

Chain	Residue	Details
E	GLU331

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000305\|PubMed:8395513

Chain	Residue	Details
E	ILE339

site_id	SWS_FT_FI10
Number of Residues	1
Details	LIPID: N-myristoyl glycine => ECO:0000269\|PubMed:11141074

Chain	Residue	Details
E	ASN2

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	GLU170
E	ASP166

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	ASP166
E	LYS168

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	THR201
E	ASP166
E	LYS168

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	ASP166
E	ASN171
E	LYS168

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