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3Q9Y

Crystal structure of human CK2 alpha in complex with Quinalizarin at pH 8.5

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 Residues8
DetailsBINDING SITE FOR RESIDUE TXQ A 337
ChainResidue
ALEU45
AVAL53
AVAL66
ALYS68
APHE113
AILE174
AASP175
AHOH347

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 338
ChainResidue
AARG278
AARG306
ATYR307
AASP308
AHOH448
AHOH450
AHOH466
AASP253

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 339
ChainResidue
ALYS77
AARG80
AARG155
AASN189
AHOH390

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 340
ChainResidue
AARG191
ALYS198
AASN238

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 Residues285
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsRegion: {"description":"Interaction with beta subunit","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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