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4DGM

Crystal Structure of maize CK2 in complex with the inhibitor apigenin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004676molecular_function3-phosphoinositide-dependent protein kinase activity
A0004677molecular_functionDNA-dependent protein kinase activity
A0004679molecular_functionAMP-activated protein kinase activity
A0004694molecular_functioneukaryotic translation initiation factor 2alpha kinase activity
A0004711molecular_functionribosomal protein S6 kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0005956cellular_componentprotein kinase CK2 complex
A0006338biological_processchromatin remodeling
A0006468biological_processprotein phosphorylation
A0006974biological_processDNA damage response
A0035175molecular_functionhistone H3S10 kinase activity
A0035402molecular_functionhistone H3T11 kinase activity
A0035403molecular_functionhistone H3T6 kinase activity
A0035979molecular_functionhistone H2AXS139 kinase activity
A0044022molecular_functionhistone H3S28 kinase activity
A0044023molecular_functionhistone H4S1 kinase activity
A0044024molecular_functionhistone H2AS1 kinase activity
A0044025molecular_functionhistone H2BS14 kinase activity
A0051726biological_processregulation of cell cycle
A0072354molecular_functionhistone H3T3 kinase activity
A0072371molecular_functionhistone H2AS121 kinase activity
A0072518molecular_functionRho-dependent protein serine/threonine kinase activity
A0106310molecular_functionprotein serine kinase activity
A0140823molecular_functionhistone H2BS36 kinase activity
A0140855molecular_functionhistone H3S57 kinase activity
A0140857molecular_functionhistone H3T45 kinase activity
A1990244molecular_functionhistone H2AT120 kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 401
ChainResidue
ATYR125
AMET221
AGLY224
AMET225
AGLU230
AHOH659

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
AHIS291
AHIS291
AHOH553
ATHR129
AASP130
AASP130

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
AVAL11
ASER212
AMET215
AARG312
ALEU313
ATHR314
AHOH516
AHOH634
AHOH635

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
AALA9
ATYR12
AALA13
AASP14
AGLN325

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEG A 405
ChainResidue
AARG278
AASP302
ALEU305
AARG306
ATYR307
AASP308
AGLU311
AHOH592

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AGI A 406
ChainResidue
AVAL45
AVAL53
AILE66
ALYS68
APHE113
AVAL116
AASN118
AMET163
AILE174
AASP175
AHOH501
AHOH581

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGKYSEVFeGinvnnnek..........CIIK
ChainResidueDetails
AVAL45-LYS68

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI
ChainResidueDetails
AILE152-ILE164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP156

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AVAL45
ALYS68

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PDB entries from 2025-02-05

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