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5OTY

The crystal structure of CK2alpha in complex with CAM4712

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 Residues3
Detailsbinding site for residue ACT A 401
ChainResidue
AARG80
AARG155
ALEU178

site_idAC2
Number of Residues3
Detailsbinding site for residue ACT A 402
ChainResidue
AGLY91
AASN93
AARG172

site_idAC3
Number of Residues4
Detailsbinding site for residue ACT A 403
ChainResidue
AHOH527
AASP103
AALA110
AARG280

site_idAC4
Number of Residues5
Detailsbinding site for residue TFA A 404
ChainResidue
ALYS68
APHE113
AILE174
AASP175
AHOH543

site_idAC5
Number of Residues11
Detailsbinding site for residue AUW A 405
ChainResidue
AASN118
APHE121
ATYR125
AMET137
APRO159
AHIS160
AVAL162
AMET163
AMET221
AMET225
AHOH576

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues33
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnnekvvvkilkpv.AAAK
ChainResidueDetails
ALEU45-LYS77

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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