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5X3F

Crystal structure of the YgjG-Protein A-Zpa963-PKA catalytic domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008483molecular_functiontransaminase activity
A0009447biological_processputrescine catabolic process
A0016740molecular_functiontransferase activity
A0019161molecular_functiondiamine transaminase activity
A0019477biological_processL-lysine catabolic process
A0019865molecular_functionimmunoglobulin binding
A0030170molecular_functionpyridoxal phosphate binding
A0033094molecular_functionputrescine--2-oxoglutarate transaminase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000166molecular_functionnucleotide binding
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
B0005929cellular_componentcilium
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
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016607cellular_componentnuclear speck
B0016740molecular_functiontransferase activity
B0018105biological_processpeptidyl-serine phosphorylation
B0019865molecular_functionimmunoglobulin binding
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0021904biological_processdorsal/ventral neural tube patterning
B0030007biological_processintracellular potassium ion homeostasis
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
B0042995cellular_componentcell projection
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
B0050766biological_processpositive regulation of phagocytosis
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
BLEU188-LYS211

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI
ChainResidueDetails
BLEU301-ILE313

site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. MIlDEVqt.GMgRtGkmfacehenvqp....DILclAKalgGG
ChainResidueDetails
AMET268-GLY305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
BASP305
AGLN274

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BLEU188
BLYS211
BGLU260
BLYS307

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11141074, ECO:0000269|PubMed:8395513
ChainResidueDetails
BASN152

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612
ChainResidueDetails
BTHR187
BTHR334

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:22323819, ECO:0000305|PubMed:8395513
ChainResidueDetails
BSER278

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
BTPO336

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21866565
ChainResidueDetails
BTYR469

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:8395513
ChainResidueDetails
BSER477

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PDB entries from 2025-06-11

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