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6YPH

Crystal Structure of CK2alpha with Compound 2 bound

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 Residues11
Detailsbinding site for residue N5Q A 401
ChainResidue
ALEU45
AASP175
AHOH510
AGLY46
AARG47
AVAL66
ALYS68
APHE113
AVAL116
AMET163
AILE174

site_idAC2
Number of Residues14
Detailsbinding site for residue N5Q B 401
ChainResidue
BLEU45
BGLY46
BARG47
BVAL53
BVAL66
BLYS68
BPHE113
BVAL116
BHIS160
BILE174
BASP175
BHOH502
BHOH519
BHOH554

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

222415

PDB entries from 2024-07-10

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