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5OTQ

The crystal structure of CK2alpha in complex with compound 33

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 Residues7
Detailsbinding site for residue ACT A 401
ChainResidue
ALYS68
AILE95
APHE113
AILE174
AASP175
AHOH555
AHOH562

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 402
ChainResidue
AARG155
AASN189
ALYS77
AARG80

site_idAC3
Number of Residues14
Detailsbinding site for residue AUH A 403
ChainResidue
ALEU45
AGLY46
ATYR125
ATHR127
ALEU128
ATYR136
AMET137
AILE140
APRO159
AHIS160
AVAL162
AMET221
AMET225
AHOH532

site_idAC4
Number of Residues7
Detailsbinding site for residue AUH A 404
ChainResidue
AGLN36
ATYR39
ALEU41
AILE69
AASP103
ATHR108
AALA110

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

227111

PDB entries from 2024-11-06

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