Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9EDC

Reset Type-I Protein Kinase A Holoenzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0001669cellular_componentacrosomal vesicle
A0001707biological_processmesoderm formation
A0001843biological_processneural tube closure
A0002027biological_processregulation of heart rate
A0003091biological_processrenal water homeostasis
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004691molecular_functioncAMP-dependent protein kinase activity
A0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005930cellular_componentaxoneme
A0005952cellular_componentcAMP-dependent protein kinase complex
A0006338biological_processchromatin remodeling
A0006397biological_processmRNA processing
A0006611biological_processprotein export from nucleus
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A0016020cellular_componentmembrane
A0016241biological_processregulation of macroautophagy
A0016301molecular_functionkinase activity
A0016607cellular_componentnuclear speck
A0016740molecular_functiontransferase activity
A0019221biological_processcytokine-mediated signaling pathway
A0019870molecular_functionpotassium channel inhibitor activity
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0021904biological_processdorsal/ventral neural tube patterning
A0030007biological_processintracellular potassium ion homeostasis
A0030145molecular_functionmanganese ion binding
A0031410cellular_componentcytoplasmic vesicle
A0031514cellular_componentmotile cilium
A0031594cellular_componentneuromuscular junction
A0032024biological_processpositive regulation of insulin secretion
A0032703biological_processnegative regulation of interleukin-2 production
A0034237molecular_functionprotein kinase A regulatory subunit binding
A0034380biological_processhigh-density lipoprotein particle assembly
A0034605biological_processcellular response to heat
A0034704cellular_componentcalcium channel complex
A0035694biological_processmitochondrial protein catabolic process
A0036126cellular_componentsperm flagellum
A0044853cellular_componentplasma membrane raft
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0045667biological_processregulation of osteoblast differentiation
A0045722biological_processpositive regulation of gluconeogenesis
A0045879biological_processnegative regulation of smoothened signaling pathway
A0046827biological_processpositive regulation of protein export from nucleus
A0048240biological_processsperm capacitation
A0048471cellular_componentperinuclear region of cytoplasm
A0050766biological_processpositive regulation of phagocytosis
A0050804biological_processmodulation of chemical synaptic transmission
A0050850biological_processpositive regulation of calcium-mediated signaling
A0051726biological_processregulation of cell cycle
A0055117biological_processregulation of cardiac muscle contraction
A0061136biological_processregulation of proteasomal protein catabolic process
A0070062cellular_componentextracellular exosome
A0070417biological_processcellular response to cold
A0070507biological_processregulation of microtubule cytoskeleton organization
A0070613biological_processregulation of protein processing
A0071333biological_processcellular response to glucose stimulus
A0071374biological_processcellular response to parathyroid hormone stimulus
A0071377biological_processcellular response to glucagon stimulus
A0071872biological_processcellular response to epinephrine stimulus
A0086064biological_processcell communication by electrical coupling involved in cardiac conduction
A0097546cellular_componentciliary base
A0097700biological_processvascular endothelial cell response to laminar fluid shear stress
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0099103molecular_functionchannel activator activity
A0099170biological_processpostsynaptic modulation of chemical synaptic transmission
A0106310molecular_functionprotein serine kinase activity
A0120186biological_processnegative regulation of protein localization to chromatin
A0140198molecular_functionhistone H1-4S35 kinase activity
A1903779biological_processregulation of cardiac conduction
A1904262biological_processnegative regulation of TORC1 signaling
A1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
A1990044biological_processprotein localization to lipid droplet
A2000810biological_processregulation of bicellular tight junction assembly
B0000166molecular_functionnucleotide binding
B0001707biological_processmesoderm formation
B0001772cellular_componentimmunological synapse
B0004862molecular_functioncAMP-dependent protein kinase inhibitor activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005771cellular_componentmultivesicular body
B0005813cellular_componentcentrosome
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005930cellular_componentaxoneme
B0005952cellular_componentcAMP-dependent protein kinase complex
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0007507biological_processheart development
B0008603molecular_functioncAMP-dependent protein kinase regulator activity
B0010629biological_processnegative regulation of gene expression
B0019904molecular_functionprotein domain specific binding
B0030552molecular_functioncAMP binding
B0031588cellular_componentnucleotide-activated protein kinase complex
B0031594cellular_componentneuromuscular junction
B0031625molecular_functionubiquitin protein ligase binding
B0032024biological_processpositive regulation of insulin secretion
B0032991cellular_componentprotein-containing complex
B0034236molecular_functionprotein kinase A catalytic subunit binding
B0042802molecular_functionidentical protein binding
B0044853cellular_componentplasma membrane raft
B0045202cellular_componentsynapse
B0045214biological_processsarcomere organization
B0046007biological_processnegative regulation of activated T cell proliferation
B0060038biological_processcardiac muscle cell proliferation
B0071377biological_processcellular response to glucagon stimulus
B0098978cellular_componentglutamatergic synapse
B0120212cellular_componentsperm head-tail coupling apparatus
B0141162biological_processnegative regulation of cAMP/PKA signal transduction
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhkesgnh..........YAMK
ChainResidueDetails
ALEU49-LYS72
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI
ChainResidueDetails
ALEU162-ILE174
site_idPS00888
Number of Residues17
DetailsCNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VIqQGDeGDnFYVIdqG
ChainResidueDetails
BVAL162-GLY178
BILE280-GLY296
site_idPS00889
Number of Residues18
DetailsCNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGElALiygtp......RAAtVkA
ChainResidueDetails
BPHE198-ALA215
BPHE322-ALA339
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05132","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"12372837","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified 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."]}}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P05132","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified 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"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsMotif: {"description":"Pseudophosphorylation motif"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9DBC7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

PDB statisticsPDBj update infoContact PDBjnumon