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1PJK

Crystal Structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 341
ChainResidue
AARG80

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ANP A 340
ChainResidue
AGLU114
AVAL116
AASN161
AASP175
AHOH345
AHOH437
AGLY48
ALYS49
ATYR50
ASER51
AVAL53
AVAL66
ALYS68
AILE95

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnnek..........VVVK
ChainResidueDetails
ALEU45-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: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU45
ALYS68

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP156
AHIS160

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP156
ALYS158

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP156
ALYS158
ASER194

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP156
AASN161
ALYS158

222415

PDB entries from 2024-07-10

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