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3PVB

Crystal structure of (73-244)RIa:C holoenzyme of cAMP-dependent Protein kinase

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
B0005952cellular_componentcAMP-dependent protein kinase complex
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ANP A 400
ChainResidue
AGLY50
AGLU121
AVAL123
AGLU127
ALYS168
AGLU170
AASN171
ALEU173
ATHR183
AASP184
APHE327
AGLY52
AMN401
AMN402
BARG94
BALA97
ASER53
APHE54
AGLY55
AVAL57
AALA70
ALYS72
AMET120

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AASN171
AASP184
AANP400

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AASP166
AASP184
AANP400

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1
ChainResidue
BGLU200
BPRO208
BARG209
BALA210
BALA211

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

site_idPS00889
Number of Residues18
DetailsCNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGElALiygtp......RAAtVkA
ChainResidueDetails
BPHE198-ALA215

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
BLEU135
BGLU200
BARG209

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9DBC7
ChainResidueDetails
BSER99
ALYS72
AGLU121
ALYS168

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11141074, ECO:0000269|PubMed:8395513
ChainResidueDetails
ASEP10

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612
ChainResidueDetails
ATHR48
ATHR195

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:22323819, ECO:0000305|PubMed:8395513
ChainResidueDetails
ASEP139

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:22323819, ECO:0000269|PubMed:8395513, ECO:0000269|PubMed:9707564
ChainResidueDetails
ATPO197

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21866565
ChainResidueDetails
ATYR330

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:8395513
ChainResidueDetails
ASEP338

237423

PDB entries from 2025-06-11

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