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4XW4

X-ray structure of PKAc with AMPPNP, SP20, calcium ions

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0005811cellular_componentlipid droplet
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005930cellular_componentaxoneme
A0005952cellular_componentcAMP-dependent protein kinase complex
A0006338biological_processchromatin remodeling
A0006397biological_processmRNA processing
A0006468biological_processprotein phosphorylation
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0008284biological_processpositive regulation of cell population proliferation
A0010898biological_processpositive regulation of triglyceride catabolic process
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016607cellular_componentnuclear speck
A0016740molecular_functiontransferase activity
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0030007biological_processintracellular potassium ion homeostasis
A0030145molecular_functionmanganese ion binding
A0031267molecular_functionsmall GTPase binding
A0031410cellular_componentcytoplasmic vesicle
A0031514cellular_componentmotile cilium
A0031588cellular_componentnucleotide-activated protein kinase complex
A0031594cellular_componentneuromuscular junction
A0031625molecular_functionubiquitin protein ligase binding
A0031669biological_processcellular response to nutrient levels
A0032991cellular_componentprotein-containing complex
A0034237molecular_functionprotein kinase A regulatory subunit binding
A0034605biological_processcellular response to heat
A0036126cellular_componentsperm flagellum
A0038110biological_processinterleukin-2-mediated signaling pathway
A0038202biological_processTORC1 signaling
A0043457biological_processregulation of cellular respiration
A0044853cellular_componentplasma membrane raft
A0044877molecular_functionprotein-containing complex binding
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0045667biological_processregulation of osteoblast differentiation
A0045722biological_processpositive regulation of gluconeogenesis
A0045820biological_processnegative regulation of glycolytic process
A0045879biological_processnegative regulation of smoothened signaling pathway
A0046827biological_processpositive regulation of protein export from nucleus
A0048240biological_processsperm capacitation
A0048471cellular_componentperinuclear region of cytoplasm
A0048792biological_processspontaneous exocytosis of neurotransmitter
A0050766biological_processpositive regulation of phagocytosis
A0050804biological_processmodulation of chemical synaptic transmission
A0051447biological_processnegative regulation of meiotic cell cycle
A0051726biological_processregulation of cell cycle
A0051966biological_processregulation of synaptic transmission, glutamatergic
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
A0097225cellular_componentsperm midpiece
A0097546cellular_componentciliary base
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0099170biological_processpostsynaptic modulation of chemical synaptic transmission
A0106310molecular_functionprotein serine kinase activity
A0140198molecular_functionhistone H1-4S35 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
B0004862molecular_functioncAMP-dependent protein kinase inhibitor activity
B0006469biological_processnegative regulation of protein kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 401
ChainResidue
AASP184
AANP403
AHOH589
AHOH592
AHOH813
BHOH711

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AHOH587
AHOH590
AHOH591
AASN171
AASP184
AANP403

site_idAC3
Number of Residues30
Detailsbinding site for residue ANP A 403
ChainResidue
ALEU49
ATHR51
AGLY52
AVAL57
AALA70
ALYS72
AVAL104
AMET120
AGLU121
ATYR122
AVAL123
AGLU127
AGLU170
AASN171
ALEU173
ATHR183
AASP184
APHE327
ACA401
ACA402
AHOH587
AHOH588
AHOH590
AHOH591
AHOH593
AHOH673
AHOH677
AHOH741
BARG618
BHOH711

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
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P17612","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
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_FI5
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_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"21866565","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"8395513","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsSite: {"description":"Important for inhibition"}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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