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6EM7

Crystal Structure of the Protein-Kinase A catalytic subunit from Criteculus Griseus in complex with compounds RKp120 and ADP

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
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
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0030145molecular_functionmanganese ion binding
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
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
D0004862molecular_functioncAMP-dependent protein kinase inhibitor activity
D0006469biological_processnegative regulation of protein kinase activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP166

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU49
ALYS72
AGLU121
ALYS168

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Deamidated asparagine => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
AASN2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132
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:0000250|UniProtKB:P05132
ChainResidueDetails
ASEP139

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517
ChainResidueDetails
ATPO197

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
ATYR330

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00517
ChainResidueDetails
ASEP338

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000250|UniProtKB:P17612
ChainResidueDetails
AGLY1

227561

PDB entries from 2024-11-20

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