Structure of PDB 4dgm Chain A

Receptor sequence
>4dgmA (length=326) Species: 4577 (Zea mays) [Search protein sequence]
SKARVYADVNVLRPKEYWDYEALTVQWGEQDDYEVVRKVGRGKYSEVFEG
INVNNNEKCIIKILKPVKKKKIKREIKILQNLMGGPNIVKLLDIVRDQHS
KTPSLIFEYVNNTDFKVLYPTLTDYDIRYYIYELLKALDYCHSQGIMHRD
VKPHNVMIDHELRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDL
QDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNHDQLVKIAKVLGTDGLNV
YLNKYRIELDPQLEALVGRHSRKPWLKFMNADNQHLVSPEAIDFLDKLLR
YDHQERLTALEAMTHPYFQQVRAAEN
3D structure
PDB4dgm Inhibition of protein kinase CK2 by flavonoids and tyrphostins. A structural insight.
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D156 K158 N161 D175 S194
Catalytic site (residue number reindexed from 1) D150 K152 N155 D169 S188
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 AGI A V45 I66 K68 F113 V116 N118 M163 I174 D175 V39 I60 K62 F107 V110 N112 M157 I168 D169 MOAD: ic50=1.2uM
PDBbind-CN: -logKd/Ki=5.92,IC50=1.2uM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
GO:0044024 histone H2AS1 kinase activity
GO:0106310 protein serine kinase activity
Biological Process
GO:0006338 chromatin remodeling
GO:0006468 protein phosphorylation
GO:0016310 phosphorylation
GO:0051726 regulation of cell cycle
Cellular Component
GO:0005634 nucleus
GO:0005829 cytosol
GO:0005956 protein kinase CK2 complex
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4dgm, PDBe:4dgm, PDBj:4dgm
PDBsum4dgm
PubMed22794353
UniProtP28523|CSK2A_MAIZE Casein kinase II subunit alpha (Gene Name=ACK2)

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