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7XYH

Crystal structure of CK2a2 complexed with AG1112

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0001669cellular_componentacrosomal vesicle
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005956cellular_componentprotein kinase CK2 complex
A0006302biological_processdouble-strand break repair
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0007283biological_processspermatogenesis
A0016055biological_processWnt signaling pathway
A0021987biological_processcerebral cortex development
A0031519cellular_componentPcG protein complex
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0051726biological_processregulation of cell cycle
A0097421biological_processliver regeneration
A0106310molecular_functionprotein serine kinase activity
A1901524biological_processregulation of mitophagy
A1903955biological_processpositive regulation of protein targeting to mitochondrion
A1905818biological_processregulation of chromosome separation
A2001234biological_processnegative regulation of apoptotic signaling pathway
B0000785cellular_componentchromatin
B0001669cellular_componentacrosomal vesicle
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005956cellular_componentprotein kinase CK2 complex
B0006302biological_processdouble-strand break repair
B0006468biological_processprotein phosphorylation
B0006915biological_processapoptotic process
B0007283biological_processspermatogenesis
B0016055biological_processWnt signaling pathway
B0021987biological_processcerebral cortex development
B0031519cellular_componentPcG protein complex
B0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
B0051726biological_processregulation of cell cycle
B0097421biological_processliver regeneration
B0106310molecular_functionprotein serine kinase activity
B1901524biological_processregulation of mitophagy
B1903955biological_processpositive regulation of protein targeting to mitochondrion
B1905818biological_processregulation of chromosome separation
B2001234biological_processnegative regulation of apoptotic signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnner..........VVVK
ChainResidueDetails
ALEU46-LYS69

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI
ChainResidueDetails
AILE153-ILE165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP157
BASP157

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU46
ALYS69
BLEU46
BLYS69

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATYR13
BTYR13

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER18
BSER18

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER21
ASER288
BSER21
BSER288

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS97
BLYS97

220113

PDB entries from 2024-05-22

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