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4IAZ

Structure of cAMP dependent protein kinase A in complex with high Ba2+ concentration, ADP and phosphorylated peptide pSP20

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
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
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
A0016607cellular_componentnuclear speck
A0018105biological_processpeptidyl-serine phosphorylation
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
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
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
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
S0004862molecular_functioncAMP-dependent protein kinase inhibitor activity
S0006469biological_processnegative regulation of protein kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BA A 401
ChainResidue
AASP184
AADP403
AHOH1003
AHOH1004
AHOH1005
SSEP621
SHOH703

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BA A 402
ChainResidue
AADP403
AHOH1002
SHOH701
SHOH702
AASN171
AASP184

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ADP A 403
ChainResidue
ALEU49
AGLY50
AGLY52
ASER53
AVAL57
AALA70
ALYS72
AGLU121
ATYR122
AVAL123
AGLU127
AGLU170
AASN171
ALEU173
AASP184
APHE327
ABA401
ABA402
AHOH1001
AHOH1006
AHOH1007
AHOH1063
AHOH1151
SARG618
SHOH704

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 Residues3
DetailsSITE: Important for inhibition => ECO:0000250
ChainResidueDetails
SARG615
SARG618
SARG619

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ALEU49
ALYS72
AGLU121
ALYS168

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:11141074
ChainResidueDetails
AASN2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11141074, ECO:0000269|PubMed:8395513
ChainResidueDetails
ASER10

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612
ChainResidueDetails
ATHR48
ATHR195

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:22323819, ECO:0000305|PubMed:8395513
ChainResidueDetails
ASEP139

site_idSWS_FT_FI7
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_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21866565
ChainResidueDetails
ATYR330

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:8395513
ChainResidueDetails
ASEP338

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:11141074
ChainResidueDetails
AGLY1

229183

PDB entries from 2024-12-18

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