Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1JLU

Crystal Structure of the Catalytic Subunit of cAMP-dependent Protein Kinase Complexed with a Phosphorylated Substrate Peptide and Detergent

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	0004679	molecular_function	AMP-activated protein 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	0008284	biological_process	positive regulation of cell population proliferation
E	0010737	biological_process	protein kinase A signaling
E	0016020	cellular_component	membrane
E	0016301	molecular_function	kinase activity
E	0016310	biological_process	phosphorylation
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	0030145	molecular_function	manganese ion binding
E	0031267	molecular_function	small GTPase 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	0032991	cellular_component	protein-containing complex
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	0043197	cellular_component	dendritic spine
E	0043457	biological_process	regulation of cellular respiration
E	0044853	cellular_component	plasma membrane raft
E	0044877	molecular_function	protein-containing complex binding
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	0048792	biological_process	spontaneous exocytosis of neurotransmitter
E	0050804	biological_process	modulation of chemical synaptic transmission
E	0051447	biological_process	negative regulation of meiotic cell cycle
E	0051726	biological_process	regulation of cell cycle
E	0051966	biological_process	regulation of synaptic transmission, glutamatergic
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	0098793	cellular_component	presynapse
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	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
S	0004862	molecular_function	cAMP-dependent protein kinase inhibitor activity
S	0006469	biological_process	negative regulation of protein kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OCT E 381

Chain	Residue
E	PHE18
E	GLU155

site_id	AC2
Number of Residues	36
Details	BINDING SITE FOR CHAIN S OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, MUSCLE/BRAIN FORM

Chain	Residue
E	GLU170
E	ASP184
E	PHE187
E	ARG190
E	VAL191
E	LYS192
E	LEU198
E	CYS199
E	GLY200
E	THR201
E	GLU203
E	GLU230
E	TYR235
E	PHE239
E	ALA240
E	ASP241
E	TYR330
E	GLU349
E	HOH407
E	HOH419
E	GLN84
S	HOH401
S	HOH422
S	HOH425
S	HOH429
S	HOH442
S	HOH450
S	HOH455
S	HOH485
S	HOH497
E	ARG93
E	GLU127
E	PHE129
E	ARG133
E	ASP166
E	LYS168

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	5
Details	SITE: Important for inhibition => ECO:0000250

Chain	Residue	Details
S	THR372
S	ARG375
S	ALA376
S	ARG371
S	ARG374

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)