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3TNQ

Structure and Allostery of the PKA RIIb Tetrameric Holoenzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0001932biological_processregulation of protein phosphorylation
A0004862molecular_functioncAMP-dependent protein kinase inhibitor activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005952cellular_componentcAMP-dependent protein kinase complex
A0006631biological_processfatty acid metabolic process
A0007612biological_processlearning
A0008603molecular_functioncAMP-dependent protein kinase regulator activity
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0030425cellular_componentdendrite
A0030552molecular_functioncAMP binding
A0031625molecular_functionubiquitin protein ligase binding
A0034236molecular_functionprotein kinase A catalytic subunit binding
A0043025cellular_componentneuronal cell body
A0043197cellular_componentdendritic spine
A0043198cellular_componentdendritic shaft
A0048471cellular_componentperinuclear region of cytoplasm
A0050804biological_processmodulation of chemical synaptic transmission
A0097332biological_processresponse to antipsychotic drug
A0097546cellular_componentciliary base
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
B0000287molecular_functionmagnesium ion binding
B0001669cellular_componentacrosomal vesicle
B0001707biological_processmesoderm formation
B0001843biological_processneural tube closure
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004679molecular_functionAMP-activated protein kinase activity
B0004691molecular_functioncAMP-dependent protein kinase activity
B0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005813cellular_componentcentrosome
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005930cellular_componentaxoneme
B0005952cellular_componentcAMP-dependent protein kinase complex
B0006397biological_processmRNA processing
B0006468biological_processprotein phosphorylation
B0006611biological_processprotein export from nucleus
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0008284biological_processpositive regulation of cell population proliferation
B0010737biological_processprotein kinase A signaling
B0016607cellular_componentnuclear speck
B0018105biological_processpeptidyl-serine phosphorylation
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0030145molecular_functionmanganese ion binding
B0031267molecular_functionsmall GTPase binding
B0031410cellular_componentcytoplasmic vesicle
B0031514cellular_componentmotile cilium
B0031588cellular_componentnucleotide-activated protein kinase complex
B0031594cellular_componentneuromuscular junction
B0031625molecular_functionubiquitin protein ligase binding
B0032024biological_processpositive regulation of insulin secretion
B0032991cellular_componentprotein-containing complex
B0034237molecular_functionprotein kinase A regulatory subunit binding
B0034605biological_processcellular response to heat
B0036126cellular_componentsperm flagellum
B0043197cellular_componentdendritic spine
B0043457biological_processregulation of cellular respiration
B0044853cellular_componentplasma membrane raft
B0044877molecular_functionprotein-containing complex binding
B0045667biological_processregulation of osteoblast differentiation
B0045722biological_processpositive regulation of gluconeogenesis
B0045879biological_processnegative regulation of smoothened signaling pathway
B0046827biological_processpositive regulation of protein export from nucleus
B0048240biological_processsperm capacitation
B0048471cellular_componentperinuclear region of cytoplasm
B0048792biological_processspontaneous exocytosis of neurotransmitter
B0050804biological_processmodulation of chemical synaptic transmission
B0051447biological_processnegative regulation of meiotic cell cycle
B0051726biological_processregulation of cell cycle
B0051966biological_processregulation of synaptic transmission, glutamatergic
B0061136biological_processregulation of proteasomal protein catabolic process
B0070417biological_processcellular response to cold
B0070613biological_processregulation of protein processing
B0071333biological_processcellular response to glucose stimulus
B0071374biological_processcellular response to parathyroid hormone stimulus
B0071377biological_processcellular response to glucagon stimulus
B0097546cellular_componentciliary base
B0098793cellular_componentpresynapse
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0099170biological_processpostsynaptic modulation of chemical synaptic transmission
B0106310molecular_functionprotein serine kinase activity
B0141156biological_processcAMP/PKA signal transduction
B1904262biological_processnegative regulation of TORC1 signaling
B1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
B1990044biological_processprotein localization to lipid droplet
B2000810biological_processregulation of bicellular tight junction assembly
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
ASEP112
BASN171
BASP184
BADP400

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
ASEP112
BASP184
BADP400

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADP B 400
ChainResidue
BVAL57
BALA70
BLYS72
BMET120
BGLU121
BTYR122
BVAL123
BGLU127
BGLU170
BASN171
BLEU173
BTHR183
BASP184
BPHE327
BMG401
BMG402
ASEP112
BGLY52

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhkesgnh..........YAMK
ChainResidueDetails
BLEU49-LYS72

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI
ChainResidueDetails
BLEU162-ILE174

site_idPS00888
Number of Residues17
DetailsCNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VIdQGDdGDnFYVIdrG
ChainResidueDetails
AVAL179-GLY195
AILE301-GLY317

site_idPS00889
Number of Residues18
DetailsCNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGElALvtnkp......RAAsAhA
ChainResidueDetails
APHE348-ALA365

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
BASP166
APHE274

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU49
BLYS72
BGLU121
BLYS168

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:9521123
ChainResidueDetails
BASN2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
BSEP10

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612
ChainResidueDetails
BTHR48
BTHR195

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
BSEP139

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517
ChainResidueDetails
BTPO197

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
BTYR330

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
BSEP338

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:9521123
ChainResidueDetails
BGLY1

222926

PDB entries from 2024-07-24

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