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5OTZ

The crystal structure of CK2alpha in complex with compound 1

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
AHOH668

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 402
ChainResidue
AASP103
AALA110
AARG280
AHOH600

site_idAC3
Number of Residues5
Detailsbinding site for residue TFA A 403
ChainResidue
AILE174
AASP175
AHOH584
ALYS68
APHE113

site_idAC4
Number of Residues10
Detailsbinding site for residue AUT A 404
ChainResidue
APHE121
ALEU124
ATYR125
AMET137
APRO159
AVAL162
AMET221
AMET225
AHOH654
AHOH669

site_idAC5
Number of Residues1
Detailsbinding site for residue AUT A 405
ChainResidue
AASN270

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
ALYS68
ALEU45

221051

PDB entries from 2024-06-12

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