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3FWQ

Inactive conformation 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
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 336
ChainResidue
AARG21
AGLU22
AGLN40
ALEU41
AASP103
AHOH364

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 337
ChainResidue
ASER311
AARG306
ATYR307
AASP308

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 338
ChainResidue
AARG80
AARG155
AGLU180
ATYR188
AASN189
AHOH498

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 339
ChainResidue
AHIS148
AALA315
AHOH399

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 340
ChainResidue
ALYS68
AILE174
AASP175
AHOH343

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 341
ChainResidue
ASER7
ATYR182
APRO184
AGLY185
AMET208

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 336
ChainResidue
BASP253
BARG278
BARG306
BTYR307
BASP308

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 337
ChainResidue
BVAL11
BHIS148
BALA315

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 338
ChainResidue
BLYS122
BPRO159
BHIS160

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 Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP156
BASP156

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU45
ALYS68
BLEU45
BLYS68

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
BASP156
BHIS160

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP156
ALYS158

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP156
BLYS158

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP156
ALYS158
ASER194

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP156
BLYS158
BSER194

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP156
AASN161
ALYS158

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP156
BASN161
BLYS158

221716

PDB entries from 2024-06-26

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