3VQH

Bromine SAD partially resolves multiple binding modes for PKA inhibitor H-89

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	0002027	biological_process	regulation of heart rate
A	0003091	biological_process	renal water homeostasis
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	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005929	cellular_component	cilium
A	0005930	cellular_component	axoneme
A	0005952	cellular_component	cAMP-dependent protein kinase complex
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	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A	0016020	cellular_component	membrane
A	0016241	biological_process	regulation of macroautophagy
A	0016301	molecular_function	kinase activity
A	0016607	cellular_component	nuclear speck
A	0016740	molecular_function	transferase activity
A	0018105	biological_process	peptidyl-serine phosphorylation
A	0019221	biological_process	cytokine-mediated signaling pathway
A	0019901	molecular_function	protein kinase binding
A	0019904	molecular_function	protein domain specific binding
A	0030007	biological_process	intracellular potassium ion homeostasis
A	0030145	molecular_function	manganese ion binding
A	0031410	cellular_component	cytoplasmic vesicle
A	0031514	cellular_component	motile cilium
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	0032703	biological_process	negative regulation of interleukin-2 production
A	0034237	molecular_function	protein kinase A regulatory subunit binding
A	0034380	biological_process	high-density lipoprotein particle assembly
A	0034605	biological_process	cellular response to heat
A	0034704	cellular_component	calcium channel complex
A	0035694	biological_process	mitochondrial protein catabolic process
A	0036126	cellular_component	sperm flagellum
A	0038110	biological_process	interleukin-2-mediated signaling pathway
A	0038202	biological_process	TORC1 signaling
A	0042995	cellular_component	cell projection
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
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	0050850	biological_process	positive regulation of calcium-mediated signaling
A	0051726	biological_process	regulation of cell cycle
A	0055117	biological_process	regulation of cardiac muscle contraction
A	0061136	biological_process	regulation of proteasomal protein catabolic process
A	0070062	cellular_component	extracellular exosome
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	0071872	biological_process	cellular response to epinephrine stimulus
A	0086064	biological_process	cell communication by electrical coupling involved in cardiac conduction
A	0097546	cellular_component	ciliary base
A	0097700	biological_process	vascular endothelial cell response to laminar fluid shear stress
A	0098794	cellular_component	postsynapse
A	0098978	cellular_component	glutamatergic synapse
A	0099103	molecular_function	channel activator activity
A	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
A	0106310	molecular_function	protein serine kinase activity
A	1903779	biological_process	regulation of cardiac conduction
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
B	0004862	molecular_function	cAMP-dependent protein kinase inhibitor activity
B	0006469	biological_process	negative regulation of protein kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE IQB A 401

Chain	Residue
A	LEU49
A	LYS72
A	LEU74
A	MET120
A	GLU121
A	TYR122
A	VAL123
A	GLU127
A	GLU170
A	ASN171
A	LEU173
A	GLY50
A	THR183
A	ASP184
A	PHE327
A	HOH501
A	HOH634
A	THR51
A	GLY52
A	PHE54
A	GLY55
A	ARG56
A	VAL57
A	ALA70

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 402

Chain	Residue
A	ARG134
A	ARG194
A	ASN326
A	PHE327
A	ASP328

---

site_id	AC3
Number of Residues	58
Details	BINDING SITE FOR CHAIN B OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA

Chain	Residue
A	SEP10
A	SER53
A	PHE54
A	LYS63
A	GLN84
A	GLU86
A	ARG93
A	GLU127
A	PHE129
A	SER130
A	ARG133
A	LYS168
A	PRO169
A	GLU170
A	PHE187
A	LYS189
A	ARG190
A	VAL191
A	LYS192
A	LEU198
A	CYS199
A	GLY200
A	PRO202
A	GLU203
A	GLU230
A	GLY234
A	TYR235
A	PRO236
A	PHE239
A	ALA240
A	ASP241
A	ILE246
A	ASP328
A	TYR330
A	GLU349
A	HOH509
A	HOH515
A	HOH522
A	HOH538
A	HOH543
A	HOH586
B	HOH101
B	HOH102
B	HOH103
B	HOH104
B	HOH105
B	HOH106
B	HOH107
B	HOH108
B	HOH109
B	HOH111
B	HOH112
B	HOH113
B	HOH114
B	HOH115
B	HOH117
B	HOH119
B	HOH120

---

Functional Information from PROSITE/UniProt

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

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"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	10
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	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}

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","evidences":[{"source":"PubMed","id":"12372837","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"12372837","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16765046","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20137943","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20481595","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20732331","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21774789","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2010","submissionDatabase":"PDB data bank","title":"Experimental active site mapping as a starting point to fragment-based lead discovery.","authors":["Behnen J.","Koester H.","Ritschel T.","Neudert G.","Heine A.","Klebe G."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P05132","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16765046","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20137943","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20481595","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20732331","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21774789","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2010","submissionDatabase":"PDB data bank","title":"Experimental active site mapping as a starting point to fragment-based lead discovery.","authors":["Behnen J.","Koester H.","Ritschel T.","Neudert G.","Heine A.","Klebe G."]}},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	3
Details	Site: {"description":"Important for inhibition","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---