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5CQU

Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with a Benzotriazole-Based Inhibitor Generated by click-chemistry

Replaces:  4BXB
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 Residues14
Detailsbinding site for residue JRJ A 401
ChainResidue
ALEU45
AVAL116
AMET163
AILE174
AASP175
AHOH587
AGLY48
ALYS49
ATYR50
ASER51
AVAL53
AVAL66
APHE113
AGLU114

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 402
ChainResidue
ALYS77
AARG80
AARG155
AASN189
AHOH531

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG191
ALYS198
AASN238
AHOH526

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 404
ChainResidue
AARG278
AARG306
ATYR307
AASP308
AHOH504

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 405
ChainResidue
AGLN36
ATYR39
AILE69
AASP103
AARG280
AHOH577

site_idAC6
Number of Residues2
Detailsbinding site for residue GOL A 406
ChainResidue
AHIS236
AASP237

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

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PDB entries from 2024-07-24

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