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2PVL

Structure-Based Design of Pyrazolo[1,5-a][1,3,5]triazine Derivatives as Potent Inhibitors of Protein Kinase CK2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0005956cellular_componentprotein kinase CK2 complex
A0006468biological_processprotein phosphorylation
A0043231cellular_componentintracellular membrane-bounded organelle
A0051726biological_processregulation of cell cycle
A0106310molecular_functionprotein serine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE P55 A 501
ChainResidue
AARG43
AILE66
APHE113
AGLU114
ATYR115
AHIS160
AMET163
AILE174
AHOH518

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGKYSEVFeGinvnnnek..........CIIK
ChainResidueDetails
AVAL45-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 Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP156

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS68
AVAL45

219140

PDB entries from 2024-05-01

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