Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2VO0

Structure of PKA-PKB chimera complexed with C-(4-(4-Chlorophenyl)-1-(7H-pyrrolo(2,3-d)pyrimidin-4-yl)piperidin-4-yl)methylamine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0001669	cellular_component	acrosomal vesicle
A	0001707	biological_process	mesoderm formation
A	0001843	biological_process	neural tube closure
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004691	molecular_function	cAMP-dependent protein kinase activity
A	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005930	cellular_component	axoneme
A	0005952	cellular_component	cAMP-dependent protein kinase complex
A	0006338	biological_process	chromatin remodeling
A	0006397	biological_process	mRNA processing
A	0006468	biological_process	protein phosphorylation
A	0006611	biological_process	protein export from nucleus
A	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
A	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016607	cellular_component	nuclear speck
A	0016740	molecular_function	transferase activity
A	0019901	molecular_function	protein kinase binding
A	0019904	molecular_function	protein domain specific binding
A	0021904	biological_process	dorsal/ventral neural tube patterning
A	0030007	biological_process	intracellular potassium ion homeostasis
A	0030145	molecular_function	manganese ion binding
A	0031594	cellular_component	neuromuscular junction
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0031669	biological_process	cellular response to nutrient levels
A	0032024	biological_process	positive regulation of insulin secretion
A	0034237	molecular_function	protein kinase A regulatory subunit binding
A	0034605	biological_process	cellular response to heat
A	0036126	cellular_component	sperm flagellum
A	0038110	biological_process	interleukin-2-mediated signaling pathway
A	0038202	biological_process	TORC1 signaling
A	0044853	cellular_component	plasma membrane raft
A	0045542	biological_process	positive regulation of cholesterol biosynthetic process
A	0045667	biological_process	regulation of osteoblast differentiation
A	0045722	biological_process	positive regulation of gluconeogenesis
A	0045879	biological_process	negative regulation of smoothened signaling pathway
A	0046827	biological_process	positive regulation of protein export from nucleus
A	0048240	biological_process	sperm capacitation
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050766	biological_process	positive regulation of phagocytosis
A	0050804	biological_process	modulation of chemical synaptic transmission
A	0051726	biological_process	regulation of cell cycle
A	0061136	biological_process	regulation of proteasomal protein catabolic process
A	0070417	biological_process	cellular response to cold
A	0070613	biological_process	regulation of protein processing
A	0071333	biological_process	cellular response to glucose stimulus
A	0071374	biological_process	cellular response to parathyroid hormone stimulus
A	0071377	biological_process	cellular response to glucagon stimulus
A	0097546	cellular_component	ciliary base
A	0098794	cellular_component	postsynapse
A	0098978	cellular_component	glutamatergic synapse
A	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
A	0106310	molecular_function	protein serine kinase activity
A	0140198	molecular_function	histone H1-4S35 kinase activity
A	1904262	biological_process	negative regulation of TORC1 signaling
A	1904539	biological_process	negative regulation of glycolytic process through fructose-6-phosphate
A	1990044	biological_process	protein localization to lipid droplet
A	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	3
Details	BINDING SITE FOR RESIDUE CL A1351

Chain	Residue
A	ASP184
A	M031354
A	HOH2169

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MRD A1352

Chain	Residue
A	ARG45
A	ILE46
A	MET58
A	GLU332
A	GLU333

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A1353

Chain	Residue
A	SER259
A	HOH2316
A	HOH2453
A	PRO258

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO I1025

Chain	Residue
I	ARG15
I	ARG18
I	ARG19
I	ASN20
I	HOH2018
I	HOH2025
I	HOH2031

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE M03 A1354

Chain	Residue
A	GLY50
A	THR51
A	GLY52
A	GLY55
A	VAL57
A	ALA70
A	THR104
A	GLU121
A	TYR122
A	ALA123
A	GLU127
A	GLU170
A	ASN171
A	MET173
A	THR183
A	ASP184
A	CL1351
A	HOH2454

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE M03 A1355

Chain	Residue
A	SEP10
A	GLU13
A	VAL15
A	PHE18
A	LEU152
A	GLU155
A	LYS292
A	TYR306
A	HOH2455
A	HOH2456

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU49-LYS72

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

Chain	Residue	Details
A	LEU162-ILE174

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6286662","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"P05132","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P17612","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05132","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"6262777","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P05132","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"6262777","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	3
Details	Site: {"description":"Important for inhibition","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU170
A	ASP166

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

Chain	Residue	Details
A	ASP166
A	LYS168

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

Chain	Residue	Details
A	THR201
A	ASP166
A	LYS168

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

Chain	Residue	Details
A	ASP166
A	ASN171
A	LYS168

site_id	MCSA1
Number of Residues	5
Details	M-CSA 757

Chain	Residue	Details
A	GLU170	activator, proton acceptor, proton donor
A	LEU172	electrostatic stabiliser, polar interaction
A	ASP175	metal ligand
A	ALA188	metal ligand
A	ILE209	electrostatic stabiliser, polar interaction

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