Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7E12

Crystal structure of PKAc-A11E complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0001669cellular_componentacrosomal vesicle
A0001707biological_processmesoderm formation
A0001843biological_processneural tube closure
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
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0005930cellular_componentaxoneme
A0005952cellular_componentcAMP-dependent protein kinase complex
A0006397biological_processmRNA processing
A0006468biological_processprotein phosphorylation
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
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016607cellular_componentnuclear speck
A0016740molecular_functiontransferase activity
A0018105biological_processpeptidyl-serine phosphorylation
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
A0031625molecular_functionubiquitin protein ligase binding
A0032024biological_processpositive regulation of insulin secretion
A0034237molecular_functionprotein kinase A regulatory subunit binding
A0034605biological_processcellular response to heat
A0036126cellular_componentsperm flagellum
A0042995cellular_componentcell projection
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
A0051726biological_processregulation of cell cycle
A0061136biological_processregulation of proteasomal protein catabolic process
A0070417biological_processcellular response to cold
A0070613biological_processregulation of protein processing
A0071333biological_processcellular response to glucose stimulus
A0071374biological_processcellular response to parathyroid hormone stimulus
A0071377biological_processcellular response to glucagon stimulus
A0097546cellular_componentciliary base
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0099170biological_processpostsynaptic modulation of chemical synaptic transmission
A0106310molecular_functionprotein serine kinase activity
A0141156biological_processcAMP/PKA signal transduction
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
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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA and DMPK","evidences":[{"source":"PubMed","id":"15598648","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22707725","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CaMK2","evidences":[{"source":"PubMed","id":"16690701","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P17612","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22323819","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8395513","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"22323819","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8395513","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9707564","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"21866565","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"8395513","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon