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1SYK

Crystal structure of E230Q mutant of cAMP-dependent protein kinase reveals unexpected apoenzyme conformation

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
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000287molecular_functionmagnesium ion binding
B0001669cellular_componentacrosomal vesicle
B0001707biological_processmesoderm formation
B0001843biological_processneural tube closure
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004691molecular_functioncAMP-dependent protein kinase activity
B0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005813cellular_componentcentrosome
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005930cellular_componentaxoneme
B0005952cellular_componentcAMP-dependent protein kinase complex
B0006397biological_processmRNA processing
B0006468biological_processprotein phosphorylation
B0006611biological_processprotein export from nucleus
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
B0016607cellular_componentnuclear speck
B0018105biological_processpeptidyl-serine phosphorylation
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0030145molecular_functionmanganese ion binding
B0031410cellular_componentcytoplasmic vesicle
B0031514cellular_componentmotile cilium
B0031594cellular_componentneuromuscular junction
B0031625molecular_functionubiquitin protein ligase binding
B0032024biological_processpositive regulation of insulin secretion
B0034237molecular_functionprotein kinase A regulatory subunit binding
B0034605biological_processcellular response to heat
B0036126cellular_componentsperm flagellum
B0044853cellular_componentplasma membrane raft
B0045542biological_processpositive regulation of cholesterol biosynthetic process
B0045667biological_processregulation of osteoblast differentiation
B0045722biological_processpositive regulation of gluconeogenesis
B0045879biological_processnegative regulation of smoothened signaling pathway
B0046827biological_processpositive regulation of protein export from nucleus
B0048240biological_processsperm capacitation
B0048471cellular_componentperinuclear region of cytoplasm
B0050804biological_processmodulation of chemical synaptic transmission
B0051726biological_processregulation of cell cycle
B0061136biological_processregulation of proteasomal protein catabolic process
B0070417biological_processcellular response to cold
B0070613biological_processregulation of protein processing
B0071333biological_processcellular response to glucose stimulus
B0071374biological_processcellular response to parathyroid hormone stimulus
B0071377biological_processcellular response to glucagon stimulus
B0097546cellular_componentciliary base
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0099170biological_processpostsynaptic modulation of chemical synaptic transmission
B0106310molecular_functionprotein serine kinase activity
B0141156biological_processcAMP/PKA signal transduction
B1904262biological_processnegative regulation of TORC1 signaling
B1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
B1990044biological_processprotein localization to lipid droplet
B2000810biological_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 Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ALEU167
BLEU167

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLY50
AILE73
ATYR122
APRO169
BGLY50
BILE73
BTYR122
BPRO169

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:11141074
ChainResidueDetails
AALA3
BALA3

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11141074, ECO:0000269|PubMed:8395513
ChainResidueDetails
AGLU11
BGLU11

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612
ChainResidueDetails
ALEU49
ATRP196
BLEU49
BTRP196

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:22323819, ECO:0000305|PubMed:8395513
ChainResidueDetails
AGLU140
BGLU140

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:22323819, ECO:0000269|PubMed:8395513, ECO:0000269|PubMed:9707564
ChainResidueDetails
ALEU198
BLEU198

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21866565
ChainResidueDetails
AGLU331
BGLU331

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:8395513
ChainResidueDetails
AILE339
BILE339

site_idSWS_FT_FI10
Number of Residues2
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:11141074
ChainResidueDetails
AASN2
BASN2

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AGLU170
AASP166

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BGLU170
BASP166

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP166
ALYS168

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP166
BLYS168

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR201
AASP166
ALYS168

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR201
BASP166
BLYS168

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP166
AASN171
ALYS168

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP166
BASN171
BLYS168

227111

PDB entries from 2024-11-06

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