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5OUM

The crystal structure of CK2alpha in complex with compound 21

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 ACT A 401
ChainResidue
ALYS68
AILE95
APHE113
AILE174
AASP175
AHOH592

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 402
ChainResidue
AHOH585
AHIS276
ASER277
ALYS279

site_idAC3
Number of Residues4
Detailsbinding site for residue ACT A 403
ChainResidue
AARG195
ATYR196
AHIS234
AGLY235

site_idAC4
Number of Residues9
Detailsbinding site for residue AVK A 404
ChainResidue
AASN118
APHE121
ATYR136
APRO159
AHIS160
AVAL162
AILE164
AMET221
AMET225

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnnek..........VVVK
ChainResidueDetails
BLEU45-LYS68

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI
ChainResidueDetails
BILE152-ILE164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
BASP156
AASP156

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

222036

PDB entries from 2024-07-03

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